Juxtaposition of signal-peptide charge and core region hydrophobicity is critical for functional signal peptides

Archives of Microbiology

Volumn 178, Issue 4, 2002, Pages 306-310

  Rusch, Sharyn L ^a,b   Mascolo, Cynthia L ^a   Kebir, Maha O ^a   Kendall, Debra A ^a  

^a UNIVERSITY OF CONNECTICUT   (United States)

^b ASTRAZENECA   (United Kingdom)

Author keywords

Hydrophobicity; Protein transport; SecA; Signal peptide

Indexed keywords

MUTANT PROTEIN; SIGNAL PEPTIDE;

AMINO TERMINAL SEQUENCE; ARTICLE; ELECTRICITY; ESCHERICHIA COLI; HYDROPHOBICITY; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN TRANSPORT;

ADENOSINE TRIPHOSPHATASES; ALKALINE PHOSPHATASE; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROPHOBICITY; MEMBRANE TRANSPORT PROTEINS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN PRECURSORS; PROTEIN SORTING SIGNALS; PROTEIN TRANSPORT;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0036039828     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-002-0453-z     Document Type: Article

References (30)

1. SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli
2. Polymeric sequences reveal a functional interrelationship between hydrophobicity and length of signal peptides
3. Titration of protein transport activity by incremental changes in signal peptide hydrophobicity
4. Effects of total hydrophobicity and length of the hydrophobic domain of a signal peptide on in vitro translocation efficiency
5. The requirement of a positive charge at the amino terminus can be compensated for by a longer central hydrophobic stretch in the functioning of signal peptides
6. Signal peptides: Exquisitely designed transport promoters
7. Physical and conformational properties of synthetic idealized signal sequences parallel their biological function
8. The amino-terminal charge and core region hydrophobicity interdependently contribute to the function of signal sequences
9. Signal peptide cleavage regions: Functional limits on length and topological implications
10. SecA specificity for different signal peptides
11. Mode of insertion of the signal sequence of a bacterial precursor protein into phospholipid bilayers as revealed by cysteine-based site-directed spectroscopy
12. A functional decaisoleucine-containing signal sequence
13. Idealization of the hydrophobic segment of the alkaline phosphatase signal peptide
14. Cleavage of structural proteins during the assembly of the head of bacteriophage T4
15. Functional limits of conformation, hydrophobicity, and steric constraints in prokaryotic signal peptide cleavage regions
16. Synthetic signal peptides specifically recognize SecA and stimulate ATPase activity in the absence of preprotein
17. The Sec protein-translocation pathway
18. The hydrophobic region of signal peptides is involved in the interaction with membrane-bound SecA
19. Culture medium for enterobacteria
20. Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery
21. Analysis of mutational alterations in the hydrophilic segment of the maltose-binding protein signal peptide
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23. DNA sequencing with chain-terminating inhibitors
24. Early events in preprotein recognition in E. coli: Interaction of SRP and trigger factor with nascent polypeptides
25. Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition particle and trigger factor
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27. Orientation of LamB signal peptides in bilayers: Influence of lipid probes on peptide binding and interpretation of fluorescence quenching data
28. Signal peptide determinants of SecA binding and stimulation of ATPase activity