Export of Protein: A Biochemical View
Annual Review of MicrobiologyPublished 1 October 1987
Linda L. Randall, S. J. S. Hardy, J R Thom
Citations184
SJR quartileQ1
SJR score4.50
SNIP2.79
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TL;DR
The role of Cl,eavage is explored in the development of the ProceSSing Site and the role of Membrane Proteins is examined in the implementation of the scheme.
Abstract
Microbiology began as a unified science using the principles of chemistry to understand living systems. The unified view quickly split into the subdisciplines of medical microbiology, molecular biology, and environmental microbiology. The advent of a ...Read More
Keywords
Biochemistry, Genetics and Molecular BiologyNursing
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NatureSecretory protein translocation across membranes—the role of the ‘docking protein’
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CellTransport of proteins into mitochondria: Translocational intermediates spanning contact sites between outer and inner membranes
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CellIn vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent post-translational translocation of the prepro-α-factor
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Journal of Biological ChemistrySequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope.
306 Citations1983Paul Wolfe, William Wickner +1 more
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The Journal of Cell BiologyProteins of rough microsomal membranes related to ribosome binding. I. Identification of ribophorins I and II, membrane proteins characteristics of rough microsomes
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NatureMutations which alter the function of the signal sequence of the maltose binding protein of Escherichia coli
270 Citations1980Huges Bedouelle, P J Bassford +4 more
Using DNA sequencing, the precise nature of mutations in the signal sequence which prevent the export of the maltose binding protein are determined, causing it to accumulate in the cytoplasm in its precursor form.
Journal of Biological ChemistryAccumulation of glyceride-containing precursor of the outer membrane lipoprotein in the cytoplasmic membrane of Escherichia coli treated with globomycin.
268 Citations1980Musaddeq Hussain, Shigeyuki Ichihara +1 more
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Journal of BacteriologyEvidence for specificity at an early step in protein export in Escherichia coli
268 Citations1985Carol A. Kumamoto, Jon Beckwith
The isolation of mutants in which the activity of the secB gene was eliminated suggest that thesecB product acts at an early step in the export process and is involved in the Export of only a subset of cell envelope proteins.
Proceedings of the National Academy of SciencesPost-translational cleavage of presecretory proteins with an extract of rough microsomes from dog pancreas containing signal peptidase activity.
262 Citations1977Robert Jackson, Günter Blobel
The protease(s) responsible for removing the amino-terminal extension of nascent presecretory proteins (signal peptidase) has been extracted from rough microsomes of dog pancreas with the detergent sodium deoxycholate and it is concluded that the signal peptid enzyme activity is confined to the rough endoplasmic reticulum and is latent.
Journal of Biological ChemistryEffects of two sec genes on protein assembly into the plasma membrane of Escherichia coli.
219 Citations1985Paul Wolfe, M. G. Rice +1 more
The requirement for sec function for export does not correlate with the presence or absence of leader peptide or with a particular subcellular compartment, but rather is specific to each particular protein.
CellSecretion in yeast: Reconstitution of the translocation and glycosylation of α-factor and invertase in a homologous cell-free system
216 Citations1986Jonathan Rothblatt, David I. Meyer
A homologous cell-free system has been derived from the yeast Saccharomyces cerevisiae that allows the translation, translocation, and glycosylation of the precursors of yeast mating factor alpha and invertase.
The EMBO JournalA defined mutation in the protein export gene within the spc ribosomal protein operon of Escherichia coli: isolation and characterization of a new temperature‐sensitive secY mutant.
216 Citations1984Kiyotaka Shiba, Koreaki Ito +2 more
It is demonstrated that the gene secY (prlA) is essential for protein translocation across the E. coli cytoplasmic membrane.
CellDifferent exported proteins in E. coli show differences in the temporal mode of processing in vivo
202 Citations1981Lars‐Göran Josefsson, Linda L. Randall
A number of exported proteins in E. coli, both periplasmic proteins and proteins of the outer membrane, were examined to determine when removal of the "signal sequence" occurs in vivo, and when processing occurred cotranslationally or post-translationally.
FEBS LettersThe cleavable prepiece of an imported mitochondrial protein is sufficient to direct cytosolic dihydrofolate reductase into the mitochondrial matrix
198 Citations1984Eduard C. Hurt, B. Pesold-Hurt +1 more
The cleavable prepiece of the precursor to yeast cytochrome c oxidase subunit IV (an imported mitochondrial protein) was attached to the amino‐terminus of mouse dihydrofolate reductase by gene fusion, and the resulting fusion protein was imported into the matrix of isolated, energized yeast mitochondria and cleaved to a polypeptide whose size was similar to that of authentic di hydrofolates reduction.
European Journal of BiochemistryOuter Membrane of <i>Salmonella</i>
186 Citations1973Peter F. Mühlradt, J Menzel +2 more
It was demonstrated in a double-label experiment that already existent, incomplete lipopolysaccharide is not completed after galactose addition but that only the newly synthesised lipopoly Saccharide carries the wild-type specificity.
Proceedings of the National Academy of SciencesRole for membrane potential in the secretion of protein into the periplasm of Escherichia coli.
174 Citations1981C J Daniels, D G Bole +2 more
A model is presented which suggests that membrane potential plays a primary role in the proper orientation of the precursor signal sequence within the membrane, thus promoting processing and secretion of periplasmic proteins.
Journal of BacteriologysecD, a new gene involved in protein export in Escherichia coli
173 Citations1987Claudette L. Gardel, S A Benson +3 more
New mutants of Escherichia coli altered in protein export were identified in phoA-lacZ and lamB- lacZ gene fusion strains by searching for mutants that showed an altered lactose phenotype, and several mutations mapped in a new gene, secD.
European Journal of BiochemistryEnergy is Required for Maturation of Exported Proteins in Escherichia coli
156 Citations1981Hans Enequist, Timothy R. Hirst +3 more
Evidence that at least one step in the export of proteins requires energy is presented, suggesting an energized membrane is probably essential for export of most periplasmic and outer membrane proteins.
Journal of Biological ChemistryCharacterization of new membrane lipoproteins and their precursors of Escherichia coli.
146 Citations1981Shigeyuki Ichihara, Musaddeq Hussain +1 more
It is suggested that the structures of the "signal" region and the mechanisms of processing of all the lipoproteins of E. coli are similar.
The Journal of Cell BiologyProteins of rough microsomal membranes related to ribosome binding. II. Cross-linking of bound ribosomes to specific membrane proteins exposed at the binding sites
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Proceedings of the National Academy of SciencesSecretion of beta-lactamase into the periplasm of Escherichia coli: evidence for a distinct release step associated with a conformational change.
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The EMBO JournalThe requirement for energy during export of beta‐lactamase in Escherichia coli is fulfilled by the total protonmotive force.
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Wild-type and pseudorevertant signal peptides of the lamB gene product of Escherichia coli interact with lipid systems whereas a nonfunctional deletion mutant signal peptide does not and conformationally related amphiphilicity and consequent membrane affinity of signal sequences are important for function in vivo.
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An alternative two‐dimensional gel procedure was developed, which proved useful for analysis of integral membrane proteins, especially in combination with detergent blotting, and showed that the gene secY specifies an integral membrane component of the protein export machinery.
Journal of Biological ChemistryLocalization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations.
121 Citations1982Scott D. Emr, P J Bassford
It is demonstrated that prlA mutations also phenotypically suppress signal sequence mutations in the malE gene encoding the periplasmic maltose-binding protein, and additional data suggest that thePrlA product directly interacts with the mutant signal sequence to restore export.
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Journal of Biological ChemistryEnergetics and intermediates of the assembly of Protein OmpA into the outer membrane of Escherichia coli.
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A multistep cyclical mechanism is proposed in which the binding of the substrate and ATP activates the protease, but the enzyme can then cleave a peptide bond, but is inactivated through ATP hydrolysis.
CellIntragenic suppressor mutations that restore export of maltose binding protein with a truncated signal peptide
106 Citations1984Vytas A. Bankaitis, Beth A. Rasmussen +1 more
The experiments suggest that the hydrophobic core region serves primarily a structural role in mediating protein secretion, and that other sequences outside of this region may be responsible for providing the initial recognition of the MBP nascent chain as a secreted protein.
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Journal of BacteriologyIntergration of the receptor for bacteriophage lambda in the outer membrane of Escherichia coli: coupling with cell division
100 Citations1975A Ryter, Howard A. Shuman +1 more
Proceedings of the National Academy of SciencesProtein export in Escherichia coli requires a soluble activity.
100 Citations1984Matthias Müller, Günter Blobel
By using a reconstituted cell-free system, the existence of a soluble activity that is required for the export of proteins in Escherichia coli is demonstrated and this export factor does not contain 6S RNA.
CellRole of the mature protein sequence of maltose-binding protein in its secretion across the E. coli cytoplasmic membrane
69 Citations1981Koreaki Ito, Jonathan Beckwith
It is suggested that the fragment may be secreted to the periplasm, but cannot assume a water-soluble conformation; the majority of the polypeptide may be associated with the external surface of the cytoplasmic membrane.
Journal of Biological ChemistryMolecular cloning and sequencing of the sppA gene and characterization of the encoded protease IV, a signal peptide peptidase, of Escherichia coli.
66 Citations1986Shigeyuki Ichihara, T Suzuki +2 more
A cross-linking study revealed that protease IV is a tetramer of the polypeptide, consistent with the deduced primary structure of the sppA gene-carrying plasmid.
Journal of Biological ChemistryPost-translational export of maltose-binding protein in Escherichia coli strains harboring malE signal sequence mutations and either prl+ or prl suppressor alleles.
63 Citations1985Jeanne P. Ryan, P J Bassford
A very rapid export process for the wild-type protein and, in contrast, a relatively slow post-translational mode of export for the altered precursor species.
Journal of Biological ChemistryProtease IV, a cytoplasmic membrane protein of Escherichia coli, has signal peptide peptidase activity.
63 Citations1984Shigeyuki Ichihara, N Beppu +1 more
It is reported that protease IV, a cytoplasmic membrane protease, exhibits the signal peptide peptidase activity and was cofractionated with proteaseIV throughout the entire process of purification of the latter enzyme.
The EMBO JournalTranslocation of nascent secretory proteins across membranes can occur late in translation.
63 Citations1986Kevin Ainger, David I. Meyer
It is demonstrated that the synthesis of secretory proteins can be uncoupled from their translocation, and that fairly large nascent chains are capable of crossing the membrane of the ER post‐translationally.
ScienceRequirement for Signal Peptide Cleavage of <i>Escherichia coli</i> Prolipoprotein
56 Citations1983Sumiko Inouye, Chian-Pin Sherman Hsu +2 more
Results indicate that stringent structural integrity at the cleavage site in the lipoprotein signal sequence is required for correct processing of prolipoprotein.
European Journal of BiochemistryNormal precursors of periplasmic proteins accumulated in the cytoplasm are not exported post‐translationally in <i>Escherichia coli</i>
50 Citations1984Jean‐Marie Pagès, Jamila Anba‐Mondoloni +4 more
Hyperproduction of phosphate-binding protein, PhoS, in strains carrying a multicopy plasmic containing the phoS gene, resulted in saturation of export sites and pre-PhoS was accumulated both in the inner membrane and in the cytoplasm.
Journal of BacteriologySuppressors of the secY24 mutation: identification and characterization of additional ssy genes in Escherichia coli
50 Citations1986Kiyotaka Shiba, Koreaki Ito +1 more
Cold-sensitive ssy mutations which suppress secY24 may define genes whose function is somehow involved in the secY-dependent protein secretion mechanism, however, the existence of multiple suppressor loci makes it unlikely that all of these genes specify additional components of the export machinery.
Current topics in membranes and transportChapter 3 The Use of Genetic Techniques to Analyze Protein Export in Escherichia coli
50 Citations1985Vytas A. Bankaitis, Jeanne P. Ryan +2 more
This chapter discusses the use of genetic techniques to analyze protein export in Escherichia coli, which lacks any kind of internal, membrane-bounded organelles.
Molecular and General Genetics MGGThe use of extragenic suppressors to define genes involved in protein export in Escherichia coli
49 Citations1984Edith Brickman, Donald Oliver +3 more
This work has characterized extragenic suppressors of a secA(Ts) mutation, previously identified by mutations which suppress signal sequence mutants, which may allow the identification of new genes involved in the export process.
Journal of BacteriologyMapping of the lipoprotein signal peptidase gene (lsp)
30 Citations1984Miguel Regué, J Remenick +3 more
A pBR322 plasmid which contains a fragment of Escherichia coli DNA encoding the lipoprotein signal peptidase gene was used to transform Hfr polA1 strains to establish that the location of the lsp gene is closely linked to that of dapB on the E. coli genetic map.
The EMBO JournalA signal sequence mutant defective in export of ribose‐binding protein and a corresponding pseudorevertant isolated without imposed selection.
28 Citations1985Akihiro Iida, James M. Groarke +5 more
Isolation of a signal sequence mutant and a corresponding pseudorevertant without specific selection or site‐directed mutagenesis emphasizes the possibility of obtaining export mutants without the use of procedures that could bias or limit the range of mutations found.
Journal of BacteriologySecretion and processing of ribose-binding protein in Escherichia coli.
23 Citations1982Jeffrey L. Garwin, Jon Beckwith
The periplasmic D-ribose-binding protein of Escherichia coli K-12 is made initially as a larger precursor form that was observed in wild-type cells and more stably in cells inhibited for protein secretion.
Journal of VirologyProcoat, the precursor of M13 coat protein, inserts post-translationally into the membrane of cells infected by wild-type virus
23 Citations1981T Date, William Wickner
In growing cells infected by wild-type coliphage M13, the synthesis of procoat protein is completed before it inserts into the plasma membrane ane is converted to coat protein.
PubMedFunctional implications of secondary structure analysis of wild type and mutant bacterial signal peptides.
17 Citations1981Hugues Bedouelle, Maurice Hofnung
Analysis of the secondary structure of several bacterial signal peptides by predictive methods shows that the predicted structures are essentially periodical and define a preferential axis, which is called the Hydrophobic Axis Length or HAL.
Proceedings of the National Academy of SciencesSecretory S complex of Bacillus subtilis forms a large, organized structure when released from ribosomes.
15 Citations1985Michael P. Caulfield, D Furlong +2 more
The S complex of Bacillus subtilis, a set of four proteins that appears to be involved in protein secretion, is shown to be attached to 70S ribosome: antibody to its 64-kDa component can aggregate these ribosomes, and the complex can be chemically crosslinked to ribosomal proteins.