SecB, a molecular chaperone with two faces

Trends in Microbiology

Volumn 9, Issue 5, 2001, Pages 193-196

  Driessen, Arnold J M ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CARRIER PROTEIN; CHAPERONE; PROTEIN PRECURSOR; PROTEIN SECA; PROTEIN SECB; PROTEIN SUBUNIT; SECRETORY PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING SITE; CELL MEMBRANE; CRYSTAL STRUCTURE; ESCHERICHIA COLI; GRAM NEGATIVE BACTERIUM; HAEMOPHILUS INFLUENZAE; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN SECRETION; PROTEIN STRUCTURE; PROTEIN TARGETING; PROTEIN TRANSPORT; REGULATORY MECHANISM;

EID: 0035339953     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0966-842X(01)01980-1     Document Type: Review

References (22)

1. Protein targeting to the bacterial cytoplasmic membrane
2. Evidence for specificity at an early step in protein export in Escherichia coli
3. - phenotype of a secB null mutant and the cold-sensitive phenotype of a secG null mutant
4. The binding of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli membrane
5. Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivo
6. A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB
7. The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation
8. Crystal structure of the bacterial protein export chaperone SecB
9. Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimers
10. Substrate specificity of the SecB chaperone
11. Calorimetric analysis of the interaction between SecB and its ligands
12. Diffusion-limited interaction between unfolded polypeptides and the Escherichia coli chaperone SecB
13. Diverse effects of mutation on the activity of the Escherichia coli export chaperone SecB
14. Modulation of folding pathways of exported proteins by the leader sequence
15. Determination of the binding frame within a physiological ligand for the chaperone SecB
16. Interaction of SecB with soluble SecA
17. The C-terminus of SecA is involved in both lipid binding and SecB binding
18. Zinc stabilizes the SecB binding site on SecA
19. Preprotein transfer to the Escherichia coli translocase requires the cooperative binding of SecB and the signal sequence to SecA
20. A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB
21. Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactions
22. SecYEG assembles into a tetramer to form the active protein translocase channel