Revised translation start site for secM defines an atypical signal peptide that regulates Escherichia coli secA expression

Journal of Bacteriology

Volumn 182, Issue 19, 2000, Pages 5592-5595

  Sarker, S ^a   Rudd, K E ^a   Oliver, D ^a  

^a WESLEYAN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; GENE PRODUCT; SIGNAL PEPTIDE;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL GENE; ESCHERICHIA COLI; GENE CONTROL; GENE EXPRESSION REGULATION; NONHUMAN; PRIORITY JOURNAL; TRANSLATION INITIATION;

ADENOSINETRIPHOSPHATASE; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CARRIER PROTEINS; CODON, INITIATOR; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENES, BACTERIAL; MOLECULAR SEQUENCE DATA; PROTEIN SORTING SIGNALS; SUPPORT, U.S. GOV'T, P.H.S.; TRANSLATION, GENETIC;

ESCHERICHIA COLI;

EID: 0033801865     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.19.5592-5595.2000     Document Type: Article

References (24)

1. SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli
2. Sequence analysis, transcriptional organization, and insertional mutagenesis of the envA gene of Escherichia coli
3. Overproduction of SecA suppresses the export defect caused by a mutation in the gene encoding the Escherichia coli export chaperone SecB
4. Competition between Sec- and TAT-dependent protein translocation in Escherichia coli
5. The Sec system
6. Distinct catalytic roles of the SecYE, SecG, and SecDFyajC subunits of preprotein translocase holoenzyme
7. The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling
8. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
9. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane
10. The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins
11. Dual regulation of Escherichia coli secA translation by distinct upstream elements
12. Synthetic signal peptides specifically recognize SecA and stimulate ATPase activity in the absence of preprotein
13. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
14. Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation
15. Regulation of Escherichia coli secA by cellular protein secretion proficiency requires an intact gene X signal sequence and an active translocon
16. Regulation of a membrane component required for protein secretion in Escherichia coli
17. The first gene in the Escherichia coli secA operon, gene X, encodes a nonessential secretory protein
18. A mutation affecting the regulation of a secA-lacZ fusion defines a new sec gene
19. Regulation of the Escherichia coli secA gene by protein secretion defects: Analysis of secA, secB, secD, and secY mutants
20. Competition between ribosome and SecA binding promotes Escherichia coli secA translational regulation
21. SecA protein autogenously represses its own translation during normal protein secretion in Escherichia coli
22. Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli
23. The catalytic cycle of the Escherichia coli SecA ATPase comprises two distinct preprotein translocation events