Authorship：Last author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：ELSEVIER SCIENCE INC  

During protein import into chloroplasts, precursor proteins are docked to these organelles under stringent energy conditions to form early translocation intermediates. Depending on the temperature and the requirement for ATP, different types of early-intermediates are present, for which the extent of precursor protein translocation differs [H. Inoue, M, Akita, J. Biol. Chem. 283 (2008) 7491-7502]. However, it has not been determined whether the environment Surrounding the precursor differs for each intermediate. We therefore employed a site-specific photo-crosslinking strategy in Our current Study to capture any components in close proximity to the targeting signal of the precursors within the early-intermediates. Various crosslinked products, one of which contains Toc75, were identified. The appearance of these products was found to be dependent on the position of the precursor upon modification by the crosslinker and also the intermediate state. This indicated that the transition of early translocation intermediates is accompanied with the movement of the targeting signal within the early-intermediates. (C) 2008 Elsevier Inc. All rights reserved.

DOI： 10.1016/j.abb.2008.06.007

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Authorship：Last author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

The in vitro protein import experiment is one of the most important techniques for determining protein localization. For chloroplastic proteins, proteins of interest are incubated with isolated chloroplasts in the presence of energy sources. Radio-labeled proteins synthesized either in vitro or in vivo have been widely used as substrate proteins. Here we report our development of the protein import assay system in which non-radio-labeled proteins, overexpressed in Escherichia coli, were applied. In this system, substrate proteins were designed to carry epitope-tags, thus allowing analysis of imported proteins by SDS-PAGE, followed by immunoblotting to detect these tags. Furthermore, the imported proteins were found to be incorporated into their native form. These observations indicated that recombinant proteins were imported into chloroplasts and folded correctly. Therefore, this assay system could represent another valuable tool for determining protein localization. © 2008 Elsevier Masson SAS. All rights reserved.

DOI： 10.1016/j.plaphy.2008.02.007

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Authorship：Last author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：American Society for Biochemistry & Molecular Biology (ASBMB)  

During the early stage of protein import into chloroplasts, precursor proteins synthesized in the cytosol irreversibly bind to chloroplasts to form the early translocation intermediate under stringent energy conditions. Many efforts have been made to identify the components involved in protein import by analyzing the early intermediate. However, the state of the precursor within the intermediate has not been well investigated so far. In this study, an attempt was made to evaluate the extent of translocation of the precursor by determining the state of the precursor in the early intermediate under various conditions and analyzing the fragments generated by limited proteolysis of the precursors docked to chloroplasts. Our results indicate that three different sets of early intermediate are formed based on temperature and the hydrolysis of GTP/ ATP. These have been identified based on the size of proteolytic fragments of the precursor as "energy-dependent association," "insertion," and "penetration" states. These findings suggest two individual ATP-hydrolyzing steps during the early stage of protein import, one of which is temperature-sensitive. Our results also demonstrate that translocation through the outer envelope membrane is mainly dependent on internal ATP.

DOI： 10.1074/jbc.m709571200

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Informa UK Limited  

Kunitz soybean trypsin inhibitor (KSTI) is hydrolyzed during seed germination to yield amino acids needed to support initial seedling growth. The type of KSTI from Glycine max (L.) Merrill cv. Toyokomachi is KSTI-Ti-b The KSTI-Ti-b from 4-day-old post-germination cotyledons (KSTI-Ti-b) has 3 or 4 amino acid residues cleaved off at the C-terminus. This KSTI modification is important to understand the mechanism of degradation in seed reserve proteins by proteases. Protease KI also cleaves amino acid residues at the C-terminus of KSTI but it removes 5 amino acid residues. Therefore, we presumed the KSTI-Ti-b was produced by a protease other than protease KI. In this study, the protease TI responsible for cleavage of KSTI-Ti-b at the C-terminus was purified. The enzyme was estimated to have a molecular mass of 33 kDa from its mobility on SDS-PAGE gels. The N-terminal amino acid sequence of the purified protease TI corresponded to amino acids Phe-73 to Phe-92 of both thiol protease isoforms A and B from the soybean leaf, and shared 83% identity with the partial amino acid sequence of the membrane-associated cysteine protease from mung bean seedlings, a protease known to perform post-translational cleavage of C-terminal peptides of target proteins. Finally, this enzyme was shown to convert KSTI-Ti-b to KSTI-Ti-b.

DOI： 10.1626/pps.10.314

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Language：English   Publishing type：Research paper (scientific journal)  

Three components of the chloroplast protein translocon, Tic110, Hsp93 (ClpC), and Tic40, have been shown to be important for protein translocation across the inner envelope membrane into the stroma. We show the molecular interactions among these three components that facilitate processing and translocation of precursor proteins. Transit-peptide binding by Tic110 recruits Tic40 binding to Tic110, which in turn causes the release of transit peptides from Tic110, freeing the transit peptides for processing. The Tic40 C-terminal domain, which is homo logous to the C terminus of cochaperones Sti1p/Hop and Hip but with no known function, stimulates adenosine triphosphate hydrolysis by Hsp93. Hsp93 dissociates from Tic40 in the presence of adenosine diphosphate, suggesting that Tic40 functions as an adenosine triphosphatase activation protein for Hsp93. Our data suggest that chloroplasts have evolved the Tic40 cochaperone to increase the efficiency of precursor processing and translocation. © The Rockefeller University Press.

DOI： 10.1083/jcb.200609172

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：AMER SOC PLANT BIOLOGISTS  

NAD is a ubiquitous coenzyme involved in oxidation-reduction reactions and is synthesized by way of quinolinate. Animals and some bacteria synthesize quinolinate from tryptophan, whereas other bacteria synthesize quinolinate from aspartate ( Asp) using L-Asp oxidase and quinolinate synthase. We show here that Arabidopsis ( Arabidopsis thaliana) uses the Asp-to-quinolinate pathway. The Arabidopsis L-Asp oxidase or quinolinate synthase gene complemented the Escherichia coli mutant defective in the corresponding gene, and T-DNA-based disruption of either of these genes, as well as of the gene coding for the enzyme quinolinate phosphoribosyltransferase, was embryo lethal. An analysis of functional green fluorescent protein-fused constructs and in vitro assays of uptake into isolated chloroplasts demonstrated that these three enzymes are located in the plastid.

DOI： 10.1104/pp.106.081091

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：SPRINGER  

The shikimate pathway is common to the biosynthesis of the three aromatic amino acids and that of various secondary metabolites in land plants. Shikimate kinase (SK; EC 2.7.1.71) catalyzes the phosphorylation of shikimate to yield shikimate 3-phosphate. In an attempt to elucidate the functional roles of enzymes that participate in the shikimate pathway in rice ( Oryza sativa), we have now identified and characterized cDNAs corresponding to three SK genes-OsSK1, OsSK2, and OsSK3-in this monocotyledenous plant. These SK cDNAs encode proteins with different NH2-terminal regions and with putative mature regions that share sequence similarity with other plant and microbial SK proteins. An in vitro assay of protein import into intact chloroplasts isolated from pea ( Pisum sativum) seedlings revealed that the full-length forms of the three rice SK proteins are translocated into chloroplasts and processed, consistent with the assumption that the different NH2-terminal sequences function as chloroplast transit peptides. The processed forms of all three rice proteins synthesized in vitro manifested SK catalytic activity. Northern blot analysis revealed that the expression of OsSK1 and OsSK2 was induced in rice calli by treatment with the elicitor N-acetylchitoheptaose, and that expression of OsSK1 and OsSK3 was up-regulated specifically during the heading stage of panicle development. These results suggest that differential expression of the three rice SK genes and the accompanying changes in the production of shikimate 3-phosphate may contribute to the defense response and to panicle development in rice.

DOI： 10.1007/s00425-005-1559-8

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：AMER SOC HORTICULTURAL SCIENCE  

Two cultivars of tulip (Tulipa gesneriana L.) were used to check the effect of trehalose-feeding on longevity of vase life. 'Oxford' plants were grown from bulbs, and trehalose-fed cut flowers were compared with the intact plants grown in pots. 'Pink Diamond' flowers were obtained commercially as cut flowers from the market, and trehalose-feeding was examined by using only flower parts. In both cultivars of plants, it was confirmed that trehalose-feeding enhanced longevity of the vase life significantly at room temperature. Additionally, mechanisms of prolonging the vase life with trehalose-fed flowers were studied by comparing the water status in the zone of elongation of tulip tepals when their growth rates were modified with different treatments. In the elongating region of tulip tepals, cell elongation rates were linearly correlated to sizes of the growth-induced water potential regardless of treatments. It was found that trehalose-feeding reduced the hydraulic conductance, resulting in a decrease in cell elongation rates. Also, trehalose helped to maintain turgor of tepal cells for longer periods. Furthermore, trehalose enhanced pigmentation in tepals, and thus, trehalose is believed to have had a role in altering the metabolism in elongating cells and in reducing hydraulic conductivity in membranes.

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Japanese Society of Agricultural, Biological and Environmental Engineers and Scientists  

The present study was undertaken to clarify the relationship between tepal growth and the hydraulic properties of expanding tulip (<I>Tulipa gesneriana</I> L.) tepals. The growth rate of outer tepals was measured with an extensiometer while growth of the tepals was altered by feeding sucrose solution or trehalose solution to cut tulip flowers. Feeding sucrose to the flowers increased cell elongation rates of tepals and feeding trehalose to the flowers decreased the cell elongation rates. Simultaneously, turgor of the epidermal cells in the zone of elongation of intact outer tepals was measured with a cell pressure probe. Cell osmotic potentials were measured with the isopiestic psychrometer after extracting cell solution of similarly treated cut flowers. Cell water potential was obtained by summing cell turgor and its osmotic potential. When the hydraulic conductance of intact growing tepal tissues was calculated by dividing the growth-induced water potentials by the relative growth rates at the steady states, it was found that the hydraulic conductance was significantly decreased by trehalose feeding. Therefore, it was thought that changes in the hydraulic conductance were responsible for rapid changes in growth rates in tulip tepals when components in the vase solution were modified in cut tulip flowers.

DOI： 10.2525/ecb1963.42.205

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Japanese Society of Agricultural, Biological and Environmental Engineers and Scientists  

Hydraulic properties related to growth of flower stalks, leaves and roots in tulip (<I>Tulipa gesneriana</I> L.) plants were studied after bulbs were stored at 20°C continuously or under low temperature for 4-, 7- or 9-week periods. The shorter cold storage periods in the bulbs resulted in the reduced growth of roots, leaves and flower stalks. Differentiation and development of vascular bundles in flower stalks of growth-reduced plants caused by the shorter cold storage periods were similar to those of rapidly growing tulip plants. A decrease in hydraulic conductance was associated solely with reduced cell elongation rates, but not with the processes of cell division and tissue differentiation. Sizes of the water potential gradient between the water source and the expanding cells were linearly related to speeds of growth rates in all organs. Further, the shortage of cold periods led to lower hydraulic conductance in the zone of elongation of those tissues. Therefore, reduced growth in the elongating zone of all tulip tissues was associated with the reduction of both the hydraulic conductance and the size of the growth-induced water potential regardless of the period of low temperature treatments.

DOI： 10.2525/ecb1963.42.193

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Wiley  

The function of Tic40 during chloroplast protein import Was investigated. Tic40 is an inner envelope membrane protein with a large hydrophilic domain located in the stroma. Arabidopsis null mutants of the atTic40 gene were very pale green and grew slowly but were not seedling lethal. Isolated mutant chloroplasts imported precursor proteins at a lower rate than wild-type chloroplasts. Mutant chloroplasts were normal in allowing binding of precursor proteins. However, during subsequent translocation across the inner membrane, fewer precursors were translocated and more precursors were released from the mutant chloroplasts. Cross-linking experiments demonstrated that Tic40 was part of the translocon complex and functioned at the same stage of import as Tic110 and Hsp93, a member of the Hsp100 family of molecular chaperones. Tertiary structure prediction and immunological studies indicated that the C-terminal portion of Tic40 contains a TPR domain followed by a domain with sequence similarity to co-chaperones Sti1p/Hop and Hip. We propose that Tic40 functions as a cochaperone in the stromal chaperone complex that facilitates protein translocation across the inner membrane.

DOI： 10.1093/emboj/cdg281

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Elsevier BV  

Transport of cytoplasmically synthesized precursor proteins into chloroplasts, like the protein transport systems of mitochondria and the endoplasmic reticulum, appears to require the action of molecular chaperones, These molecules are likely to be the sites of the ATP hydrolysis required for precursor proteins to bind to and be translocated across the two membranes of the chloroplast envelope. Over the past decade, several different chaperones have been identified, based mainly on their association with precursor proteins and/or components of the chloroplast import complex, as putative factors mediating chloroplast protein import. These factors include cytoplasmic, chloroplast envelope-associated and stromal members of the Hsp70 family of chaperones, as well as stromal Hsp100 and Hsp60 chaperones and a cytoplasmic 14-3-3 protein. While many of the findings regarding the action of chaperones during chloroplast protein import parallel those seen for mitochondrial and endoplasmic reticulum protein transport, the chloroplast import system also has unique aspects, including its hypothesized use of an Hsp100 chaperone to drive translocation into the organelle interior. Many questions concerning the specific functions of chaperones during protein import into chloroplasts still remain that future studies, both biochemical and genetic, will need to address. (C) 2001 Elsevier Science B.V. All rights reserved.

DOI： 10.1016/s0167-4889(01)00148-3

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Authorship：Lead author,　Corresponding author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Japanese Society of Agricultural, Biological and Environmental Engineers and Scientists  

HSP100/Clp family of proteins, unnoticed until quite recently, involves in various cellular activities in the various cellular locations in the living organisms. Their family proteins have been classified into subfamilies based upon their sequence similarities. Their functions are varied, e.g. to obtain the tolerance to the higher temperature, to enhance the proteolytic activity by the protease, to promote transport, and so on. It seems that even the proteins in the same subfamily in the different organisms have the different features. However, HSP100/Clp proteins have one feature in common, playing a role as a molecular chaperone utilizing ATP to accomplish these activities.

DOI： 10.2525/ecb1963.39.139

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：Rockefeller University Press  

Transport of cytoplasmically synthesized proteins into chloroplasts uses an import machinery present in the envelope membranes. To identify the components of this machinery and to begin to examine how these components interact during transport, chemical cross-linking was performed on intact chloroplasts containing precursor proteins trapped at a particular stage of transport by ATP limitation. Large crosslinked complexes were observed using three different reversible homobifunctional cross-linkers. Three outer envelope membrane proteins (OEP86, OEP75, and OEP34) and one inner envelope membrane protein (IEP110), previously reported to be involved in protein import, were identified as components of these complexes. In addition to these membrane proteins, a stromal member of the hsp100 family, ClpC, was also present in the complexes. We propose that ClpC functions as a molecular chaperone, cooperating with other components to accomplish the transport of precursor proteins into chloroplasts. We also propose that each envelope membrane contains distinct translocation complexes and that a portion of these interact to form contact sites even in the absence of precursor proteins.

DOI： 10.1083/jcb.136.5.983

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Wiley  

Cytoplasmically synthesized precursors interact with translocation components in both the outer and inner envelope membranes during transport into chloroplasts. Using co-immunoprecipitation techniques, with antibodies specific to known translocation components, we identified stable interactions between precursor proteins and their associated membrane translocation components in detergent-solubilized chloroplastic membrane fractions. Antibodies specific to the outer envelope translocation components OEP75 and OEP34, the inner envelope translocation component IEP110 and the stromal Hsp100, ClpC, specifically co-immunoprecipitated precursor proteins under limiting ATP conditions, a stage we have called docking, A portion of these same translocation components was coimmunoprecipitated as a complex, and could also be detected by co-sedimentation through a sucrose density gradient. ClpC was observed only in complexes with those precursors utilizing the general import apparatus, and its interaction with precursor-containing translocation complexes was destabilized by ATP. Finally, ClpC was co-immunoprecipitated with a portion of the translocation components of both outer and inner envelope membranes, even in the absence of added precursors. We discuss possible roles for stromal Hsp100 in protein import and mechanisms of precursor binding in chloroplasts.

DOI： 10.1093/emboj/16.5.935

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：WILEY-BLACKWELL  

Proteins from both the inner and outer envelope membranes are engaged in the recognition and translocation of precursor proteins into chloroplasts, A 110 kDa protein of the chloroplastic inner envelope membrane was identified as a component of the protein import apparatus by two methods, First, this protein was part of a 600 kDa complex generated by crosslinking of precursors trapped in the translocation process. Second, solubilization with detergents of chloroplasts containing trapped precursors resulted in the identification of a complex containing both radiolabeled precursor and IEP110, Trypsin treatment of intact purified chloroplasts was used to study the topology of IEP110. The protease treatment left the inner membrane intact while simultaneously degrading domains of inner envelope proteins exposed to the intermembrane space, About 90 kDa of IEP110 was proteolitically removed, indicating that large portions protrude into the intermembrane space, Hydropathy analysis of the protein sequence deduced from the isolated cDNA clone in addition to Western blot analysis using an antiserum of IEP110 specific to the N-terminal 20 kDa, suggests that the N-terminus serves to anchor the protein in the membrane, We speculate that IEP110 could be involved in the formation of translocation contact sites due to its specific topology.

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC  

SecA interacts with presecretory proteins through recognition of the positive charge at the amino terminus of the signal peptide (Akita, M., Sasaki, S., Matsuyama, S., and Mizushima, S. (1989) J. Biol. Chem. 265, 8164-8169). A large variety of amino-terminal and carboxyl-terminal fragments of SecA were prepared in 6 M guanidine hydrochloride. SecA analogues were then reconstituted from them and examined for their ability to cross-link with [S-35]proOmpF-Lpp, a presecretory protein, in the presence of 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide. The reconstituted SecA analogues were active in the cross-linking with proOmpF-Lpp when the SecA fragments used were large enough to structurally complement each other. The cross-linking was signal peptide-dependent and suppressed in the presence of other presecretory proteins. The cross-linking was enhanced in the presence of ATP. The SecA fragments that cross-linked with proOmpF-Lpp were then analyzed on sodium dodecyl sulfate-polyacrylamide gels. The cross-linking preferentially took place on fragments possessing the amino terminus of SecA. Weak cross-linking was also observed with carboxyl-terminal fragments when they were large enough. The smallest amino-terminal and carboxyl-terminal fragments with which the cross-linking was observed were 39 and 72 kDa, respectively. From these results, the region responsible for the cross-linking with presecretory proteins was deduced to be located between amino acid residues 267 and 340 from the amino terminus of SecA. These results are discussed in relation to the structure and function of SecA.

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)  

Size exclusion chromatography of the cytosolic fraction of SecA-overproducing cells of Escherichia coli suggested that SecA, an essential component of the secretory machinery, exists as an oligomer. The subunit structure of SecA was then studied using a purified specimen. Estimation of the molecular mass by means of ultracentrifugation and chemical cross-linking analysis revealed that SecA exists as a homodimer. The purified SecA was denatured in 6 M guanidine-HCl and renatured to a dimer, which was fully active in terms of translocation, even in the presence of 1 mM dithiothreitol. It is suggested that the dimeric structure is not critically maintained by disulfide bonding between the two subunits, each of which contains four cysteine residues. © 1991.

DOI： 10.1016/0006-291X(91)90507-4

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Language：English   Publishing type：Research paper (scientific journal)  

SecA is an essential component of the protein secretory machinery of Escherichia coli. SecA denatured in 6 M guanidine hydrochloride was quantitatively renatured through dilution and dialysis. The renatured SecA was the same as native SecA as to the CD spectrum, fluorescence spectrum for tryptophan residues and dimeric structure. It was as functionally active as native SecA as to interactions with ATP and presecretory proteins, and invitro translocation. SecA-N95, which lacks the carboxyl-terminal 70 amino acid residues including three of four cysteine residues and yet is as active as intact SecA as to in vitro translocation, was also renatured to an active form from the guanidine solution. Furthermore, the renaturation of SecA took place in the presence of 1 mM dithiothreitol. It is concluded that disulfide bridges, both intra- and intermolecular ones, do not play a role in the folding and functioning of the SecA molecule. © 1990.

DOI： 10.1016/0006-291X(90)91578-G

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC  

(R)-Trichostatin A (TSA) is a Streptomyces product which causes the induction of Friend cell differentiation and specific inhibition of the cell cycle of normal rat fibroblasts in the G1 and G2 phases at the very low concentrations. We found that TSA caused an accumulation of acetylated histone species in a variety of mammalian cell lines. Pulse-labeling experiments indicated that TSA markedly prolonged the in vivo half-life of the labile acetyl groups on histones in mouse mammary gland tumor cells, FM3A. The partially purified histone deacetylase from wild-type FM3A cells was effectively inhibited by TSA in a noncompetitive manner with Ki = 3.4 nM. A newly isolated mutant cell line of FM3A resistant to TSA did not show the accumulation of the acetylated histones in the presence of a higher concentration of TSA. The histone deacetylase preparation from the mutant showed decreased sensitivity to TSA (Ki = 31 nM, noncompetitive). These results clearly indicate that TSA is a potent and specific inhibitor of the histone deacetylase and that the in vivo effect of TSA on cell proliferation and differentiation can be attributed to the inhibition of the enzyme.

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Authorship：Lead author   Language：English   Publishing type：Research paper (scientific journal)   Publisher：AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC  

SecA is an acidic, peripheral membrane protein involved in the translocation of secretory proteins across the cytoplasmic membrane. The direct interaction of SecA with secretory proteins was demonstrated by means of chemical cross-linking with 1-ethyl-3-(3-dimethylaminoprophyl)carbodiimide. OmpF-Lpp, a model secretory protein, carries either an uncleavable or cleavable signal peptide, and mutant secretory proteins derived from uncleavable OmpF-Lpp were used as translocation substrates. The interaction was SecA-specific. None of the control proteins, which are as acidic as SecA, was cross-linked with uncleavable OmpF-Lpp. The interaction was signal peptide-dependent. The interaction was increasingly enhanced as the number of positively charged amino acid residues at the amino-terminal region of the signal peptide was increased, irrespective of the species of amino acid residues donating the charge. Finally, parallelism was observed between the efficiency of interaction and that of translocation among mutant secretory proteins. It is suggested that precursors of secretory proteins interact with SecA to initiate the translocation reaction.

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Language：English   Publishing type：Research paper (scientific journal)   Publisher：Wiley  

DOI： 10.1016/0014-5793(89)80516-2

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Language：English   Publishing type：Research paper, summary (international conference)   Publisher：OXFORD UNIV PRESS  

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Language：Japanese  

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Language：English   Publishing type：Research paper, summary (international conference)   Publisher：AMER SOC CELL BIOLOGY  

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Language：English   Publisher：SPRINGER-VERLAG BERLIN  

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Language：English   Publishing type：Research paper, summary (international conference)   Publisher：AMER SOC CELL BIOLOGY  

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Language：English   Publishing type：Research paper, summary (international conference)   Publisher：WILEY-LISS  

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