Complex behavior in solution of homodimeric SecA

Protein Science

Volumn 11, Issue 4, 2002, Pages 875-882

  Woodbury, Ronald L ^a,b   Hardy, Simon J S ^a,b   Randall, Linda L ^a,b  

^a WASHINGTON STATE UNIVERSITY   (United States)

^b University of Missouri   (United States)

Author keywords

Equilibrium constant; Homodimer; Light scatter; Protein export; SecA

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONE; DIMER; HELICASE; MESSENGER RNA; POLYPEPTIDE; PROTEIN SECA; PROTEIN SUBUNIT; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

ARTICLE; CENTRIFUGATION; COLUMN CHROMATOGRAPHY; CONCENTRATION RESPONSE; DISSOCIATION CONSTANT; EQUILIBRIUM CONSTANT; IONIC STRENGTH; LIGHT SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; TEMPERATURE SENSITIVITY;

ADENOSINE TRIPHOSPHATASES; BACTERIA; BACTERIAL PROTEINS; ESCHERICHIA COLI PROTEINS; LIGHT; MEMBRANE TRANSPORT PROTEINS; MOLECULAR WEIGHT; PROTEIN BINDING; PROTEIN PRECURSORS; SCATTERING, RADIATION; SOLUTIONS; ULTRACENTRIFUGATION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0036129188     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.4090102     Document Type: Article

References (22)

1. SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer
2. Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli
3. Coupling between the sodium and proton gradients in respiring Escherichia coli cells measured by 23Na and 31P nuclear magnetic resonance
4. Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein-DNA interactions in vivo
5. Identification and characterization of protease-resistant SecA fragments: SecA has two membrane-integral forms
6. Identification and interpretation of complexity in sedimentation velocity boundaries
7. SecA folds via a dimeric intermediate
8. SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer
9. Zinc stabilizes the SecB binding site of SecA
10. Protein targeting to the bacterial cytoplasmic membrane
11. SecA protein is directly involved in protein secretion in Escherichia coli
12. Deducing the organization of a transmembrane domain by disulfide cross-linking. The bacterial chemoreceptor Trg
13. On the role of intramolecular potassium in protein synthesis
14. SecA is required for the insertion of inner membrane proteins targeted by the Escherichia coli signal recognition particle
15. Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding
16. Cation transport in Escherichia coli. Potassium transport mutants
17. Enhancement of protein spectra with tryptophan analogs: Fluorescence spectroscopy of protein-protein and protein-nucleic acid interactions
18. Analysis of non-ideal behavior in concentrated hemoglobin solutions
19. A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery
20. Boundary analysis of sedimentation velocity experiments with monodisperse and paucidisperse solutes
21. Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactions
22. Identification of the zinc ligands in cobalamin-independent methionine synthase (MetE) from Escherichia coli