Critical regions of secM that control its translation and secretion and promote secretion-specific secA regulation

Journal of Bacteriology

Volumn 184, Issue 9, 2002, Pages 2360-2369

  Sarker, Shameema ^a   Oliver, Donald ^a  

^a WESLEYAN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; PROTEIN SECA; PROTEIN SECM; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN SECRETION; REGULATORY MECHANISM; RNA TRANSLATION; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION; TRANSLATION INITIATION; TRANSLATION REGULATION;

3' UNTRANSLATED REGIONS; ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; ENTEROBACTERIACEAE; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION REGULATION, BACTERIAL; GENES, BACTERIAL; MEMBRANE TRANSPORT PROTEINS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BIOSYNTHESIS; PROTEIN SORTING SIGNALS; SEQUENCE ALIGNMENT;

EID: 0036223671     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.184.9.2360-2369.2002     Document Type: Article

References (53)

1. SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli
2. Intragenic suppressor mutations that restore export of maltose binding protein with a truncated signal peptide
3. Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor
4. prl mutations in the Escherichia coli secG gene
5. Competition between functional signal peptides demonstrates variation in affinity for the secretion pathway
6. Polymeric sequences reveal a functional interrelationship between hydrophobicity and length of signal peptides
7. Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli
8. Titration of protein transport activity by incremental changes in signal peptide hydrophobicity
9. Structure and function of the signal peptide
10. Distinct catalytic roles of the SecYE. SecG, and SecDFyajC subunits of preprotein translocase holoenzyme
11. The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling
12. SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF
13. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
14. Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations
15. Suppressor mutations that restore export of a protein with a defective signal sequence
16. Importance of secondary structure in the signal sequence for protein secretion
17. Novel seca alleles improve export of maltose-binding protein synthesized with a defective signal peptide
18. PrlA and PrlG suppressors reduce the requirement for signal sequence recognition
19. Posttranscriptional regulatory mechanisms in Escherichia coli
20. The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane
21. Extension inhibition analysis of translation initiation complexes
22. The major proteins of the Escherichia coli outer cell envelope membrane
23. Suppression of signal sequence defects and azide resistance in Escherichia coli commonly result from the same mutations in secA
24. In vitro studies with purified components reveal signal recognition particle (SRP) and SecA/SecB as constituents of two independent protein-targeting pathways of Escherichia coli
25. Ribosome regulation by the nascent peptide
26. Escherichia coli translocase: The unraveling of a molecular machine
27. SecYEG assembles into a tetramer to form the active protein translocation channel
28. Roles of SecG and ATP- and SecA-dependent protein translocation
29. Dual regulation of Escherichia coli seca translation by distinct upstream elements
30. The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eucaryotic Sec61p complex
31. The hydrophobic region of signal peptides is involved in the interaction with membrane-bound SecA
32. Secretion monitor, SecM, undergoes self-translation arrest in the cytosol
33. Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation
34. E. coli mutant pleiotropically defective in the export of secreted proteins
35. Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery
36. Regulation of Escherichia coli seca by cellular protein secretion proficiency requires an intact gene X signal sequence and an active translocon
37. Regulation of a membrane component required for protein secretion in Escherichia coli
38. Analysis of mutational alterations in the hydrophilic segment of the maltose-binding protein signal peptide
39. SecA is required for the insertion of inner membrane proteins targeted by the Escherichia coli signal recognition particle
40. The first gene in the Escherichia coli seca operon, gene X, encodes a nonessential secretory protein
41. Identification of elements on gene X-secA RNA of Escherichia coli required for SecA binding and secA auto-regulation
42. Revised translation start site of secM defines an atypical signal peptide that regulates Escherichia coli seca expression
43. SecA protein autogenously represses its own translation during normal protein secretion in Escherichia coli
44. Nucleotide sequence of the seca gene and seca (Ts) mutations preventing protein export in Escherichia coli
45. Escherichia coli SecA helicase activity is not required in vivo for efficient protein translocation or autogenous regulation
46. SecA is not required for signal recognition particle-mediated targeting and initial membrane insertion of a nascent inner membrane protein
47. New suppressors of signal-sequence mutations, prlG, are linked tightly to the secE gene of Escherichia coli
48. The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
49. A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery
50. PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation
51. The catalytic cycle of the Escherichia coli SecA ATPase comprises two distinct preprotein translocation events
52. Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope