Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles.

Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. Abstract Text:

H Mori,H Sugiyama,M Yamanaka,K Sato,M Tagaya,S Mizushima,

Protein translocation across the cytoplasmic membrane of Escherichia coli is accomplished by concerted actions of the translocation ATPase SecA and the membrane-embedded SecE/Y/G complex. SecA interacts with preproteins and undergoes ATP-driven cycles of membrane insertion-deinsertion. To address how SecA interacts functionally with other components in the translocation machinery, we characterized a SecA mutant lacking amino-terminal 8 amino acid residues (SecA N-8). Although the absence of the 8 residues did not grossly affect the interaction of SecA with a preprotein, ATP, or phospholipids, nor did it affect the intrinsic ATPase activity, it gave differential effects on the translocation of different preproteins. It also affected the translocation ATPase activity, the ability of membrane insertion, and the topology inversion of SecG coupled with the membrane insertion-deinsertion of SecA. Most noteworthy, SecA N-8 was pronouncedly defective in the translocation of proton motive force-dependent preproteins, in which SecG might have a role. We propose that the amino-terminal region of SecA is important for the functional interaction with SecG.

Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. Publishing Authors By Initials

H Mori,H Sugiyama,M Yamanaka,K Sato,M Tagaya,S Mizushima,

For similar genetic processes: mutagenesis: sequence deletion research abstracts see: genetic processes: mutagenesis: sequence deletion research

PUBMED ID PMID:

MEDLINE DATE:

Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 124

Page Numbers: 122-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1998

Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. Keywords Mesh Terms:

KEYWORDS: Sequence Deletion

MESH TERMS: metabolism

Chemical & Substance for Abstract: Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles. Information

Substance Name: Adenosine Triphosphatases

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles.

AFFILIATION: School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo, 192-0392, Japan.

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles Related Publications

• Acidic phospholipids with unsaturated fatty acids inhibit the binding of origin recognition complex to origin DNA.
• Arrangement of bacteriophage lambda receptor protein (LamB) in the Escherichia coli cell surface.
• Arrangement of bacteriophage lambda receptor protein (LamB) in the cell surface of Escherichia coli: a reconstitution study.
• Autophagy: process and function.
• Characterization of major outer membrane proteins O-8 and O-9 of Escherichia coli K-12. Evidence that structural genes for the two proteins are different.
• Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12.
• Identification of an outer membrane protein responsible for the binding of the Fe-enterochelin complex to Escherichia coli cells.
• Inhibition of vesicle-mediated protein transport by nordihydroguaiaretic acid.
• Insertion of a signal peptide-derived hydrophobic segment into the mature domain of OmpC, an outer membrane protein, does not interfere with the export of the following polypeptide chain across the cytoplasmic membrane of E. coli.
• Interaction between ORC and Cdt1p of Saccharomyces cerevisiae.
• Interactions of outer membrane proteins O-8 and O-9 with peptidoglycan sacculus of Escherichia coli K-12.
• Involvement of outer membrane proteins in enterochelin-mediated iron uptake in Escherichia coli.
• Involvement of prostaglandin E2 in production of amyloid-beta peptides both in vitro and in vivo.
• Isolation and characterization of deletion mutants of ompR and envZ, regulatory genes for expression of the outer membrane proteins OmpC and OmpF in Escherichia coli.
• Lipoprotein-bearing peptidoglycan sacculus as a preferred site for the in vitro assembly of membrane from dissociated components of outer membrane of Escherichia coli K-12.
• Membrane ATPase of Bacillus megaterium. I. Properties of membrane ATPase and its solubilized form.
• Molecular assembly of the lipoprotein trimer on the peptidoglycan layer of Escherichia coli.
• Purification and characterization of a signal peptide, a product of protein secretion across the cytoplasmic membrane of Escherichia coli.
• Purification and properties of membrane bound NADH2 dehydrogenase in Bacillus megaterium.
• Removal by bovine serum albumin of fatty acids from membrane vesicles and its effect on proline transport activity in Escherichia coli.
• Sequence-independent DNA binding activity of DnaA protein, the initiator of chromosomal DNA replication in Escherichia coli.
• Site-directed mutational analysis of DnaA protein, the initiator of chromosomal DNA replication in E. coli.
• Spectral characteristics of yeast cytochrome c's at the temperature of liquid nitrogen.
• Strain specificity of outer membrane proteins in Escherichia coli.
• The hydrophobic region of signal peptides is a determinant for SRP recognition and protein translocation across the ER membrane.
• The membrane ATPase of Bacillus megaterium. II. Purification of membrane ATPases and their recombination with membrane.
• Use of a series of ompF-ompC chimeric proteins for locating antigenic determinants recognized by monoclonal antibodies against the ompC and ompF proteins of the Escherichia coli outer membrane.
• Yeast two-hybrid analysis of the origin recognition complex of Saccharomyces cerevisiae: interaction between subunits and identification of binding proteins.
• [Induction of HO-1 by NSAIDs and its role in NSAID-induced gastric ulcers]
• [Protection of gastrointestinal mucosa against NSAID-induced ulcer]