Protein export in Escherichia coli

Johnson, K. E.; Murphy, Christian; Beckwith, Jon

doi:10.1016/0958-1669(92)90075-t

Cited by 12 publications

(6 citation statements)

References 33 publications

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“…Consistent with this possibility, it has been shown that the SecA inhibitor, azide [45], inhibits the transport across the thylakoid membrane of two of the lumenal proteins studied: 33K and plastocyanin [34]. These results agree with the observed requirements for the transport of these proteins across the thylakoid membrane; transport of 33K and PC requires the presence of soluble factors and ATP [27,47], and secdependent translocation in bacteria likewise involves a soluble factor (the chaperone, SecB) and requires ATP (for the function of SecA, reviewed in [29]). …”

Section: Phylogeny Of the Translocation Mechanismssupporting

confidence: 70%

“…Insertion of LHCPII requires ATP and a stromal protein factor; the requirements for thylakoidal protein translocation are shown in greater detail in Fig. 3. certainly turn out to resemble the sec-dependent export mechanism, involving the participation of a soluble chaperone (SecB) and an ATPdependent translocation factor (SecA) in E. coli (reviewed in [29]). This simple view was only challenged after assays were developed for the import of proteins by isolated thylakoids.…”

Section: Distinct Mechanisms Of Thylakoidal Protein Translocationmentioning

confidence: 99%

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Targeting of proteins into and across the thylakoid membrane ? a multitude of mechanisms

Robinson

Klösgen

1994

Plant Mol Biol

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Section: Phylogeny Of the Translocation Mechanismssupporting

confidence: 70%

Section: Distinct Mechanisms Of Thylakoidal Protein Translocationmentioning

confidence: 99%

Targeting of proteins into and across the thylakoid membrane ? a multitude of mechanisms

Robinson

Klösgen

1994

Plant Mol Biol

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“…coli hydrogenases-1 (Hya) and -2 (Hyb) are membrane- 1 The abbreviations used are: PCR, polymerase chain reaction; TMAO, trimethylamine N-oxide; MGD, molybdopterin guanine dinucleotide; Fdn, formate dehydrogenase-N.…”

Section: The Export Of Five Different Cofactor-containing Proteins Ismentioning

confidence: 99%

“…1). The translocation of substrates by this system involves the participation of both cytoplasmic and membrane-bound components; the soluble components, SecB and SecA, serve to prevent folding of the protein until it is directed to the membranebound translocase, a complex of SecYEG together with several less well defined ancillary proteins.…”

mentioning

confidence: 99%

An Essential Component of a Novel Bacterial Protein Export System with Homologues in Plastids and Mitochondria

Bogsch¹,

Sargent²,

Stanley³

et al. 1998

Journal of Biological Chemistry

350

313

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Proteins are transported across the bacterial plasma membrane and the chloroplast thylakoid membrane by means of protein translocases that recognize N-terminal targeting signals in their cognate substrates. Transport of many of these proteins involves the well defined Sec apparatus that operates in both membranes. We describe here the identification of a novel component of a bacterial Sec-independent translocase. The system probably functions in a similar manner to a Sec-independent translocase in the thylakoid membrane, and substrates for both systems bear a characteristic twinarginine motif in the targeting peptide. The translocase component is encoded in Escherichia coli by an unassigned reading frame, yigU, disruption of which blocks the export of at least five twin-Arg-containing precursor proteins that are predicted to bind redox cofactors, and hence fold, prior to translocation. The Sec pathway remains unaffected in the deletion strain. The gene has been designated tatC (for twin-arginine translocation), and we show that homologous genes are present in a range of bacteria, plastids, and mitochondria. These findings suggest a central role for TatC-type proteins in the translocation of tightly folded proteins across a spectrum of biological membranes.

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“…Exported proteins face a harsher environment in the periplasm, since this space is more vulnerable to environmental stresses than is the cytosol (1). It is thus reasonable to expect that in Escherichia coli there may be periplasmic chaperones whose function is to ensure the proper folding and maintenance of periplasmic proteins.…”

mentioning

confidence: 99%

Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo.

Missiakas

Georgopoulos

Raina

1993

Proc. Natl. Acad. Sci. U.S.A.

243

242

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We have identified and characterized the Escherichia coli gene dsbB, whose product is required for diaulfide bond formation of periplasmic proteins, by using two different approaches: (i) screening of a multicopy plasmid library for clones which protect E. coli from the lethal effects of dithiothreitol (DTT), and (ii) screening of insertion libraries of E. coli for DTT-sensitive mutants. Mapping and characterization of mutations conferring a DTT-sensitive phenotype also identified the dsbA, trxA, and trxB genes, whose products are involved in different oxidation-reduction pathways. Null mutations in dsbB conferred pleiotropic phenotypes such as sensitivity to benzylpenicillin and inability to support plaque formation of filamentous phages, and they were shown to severely affect disulfide bond oxidation of secreted proteins such as OmpA and &3lactamase. These phenotypes resemble the phenotype of bacteria carrying either a null mutation in the dsbA gene or the double mutation dsbA dsbB. Sequencing and expression of the dsbB gene revealed that it encodes a 20-kDa protein predicted to possess an "exchangeable" disulfide bond in -Cys-Val-Leu-Cys-. The dsbB gene maps at 26.5 min on the genetic map of the E. coil chromosome, and its transcription is directed from two promoters, neither of which resembles the canonical Eo7'-recognized promoter.

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Protein export in Escherichia coli

Cited by 12 publications

References 33 publications

Targeting of proteins into and across the thylakoid membrane ? a multitude of mechanisms

Targeting of proteins into and across the thylakoid membrane ? a multitude of mechanisms

An Essential Component of a Novel Bacterial Protein Export System with Homologues in Plastids and Mitochondria

Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo.

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