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Title: Structure and assembly of the flagellar hook-basal body complex of Salmonella typhimurium

Abstract

The hook-basal body (HBB) complex is a multi-component structure which comprises a significant part of the bacterial flagellar motor. Electrophoretic mobility shifts of HBB complex component proteins from four non-flagellate mutants have enabled the author to assign each protein as being the product of the gene defective in each of the respective strains. The author has purified and characterized HBB complexes lacking either the L ring or both the P and L rings, and concluded that the 27-kDa basal-body protein is the major component of the L ring, and that the 38-kDa basal-body protein is the major component of the P ring. He has sequenced the genes encoding the subunit proteins of the M, P, and L rings of the basal body, and have examined both the gene and deduced amino acid sequences for clues regarding the regulation of these genes and the structure of their products. By quantitating the amount of {sup 35}S incorporated into the component protein vivo and correcting for the amount of contained in each protein (as deduced from gene sequencing data), he has determined the relative stoichiometries of most of the known component proteins of the HBB complex. He has developed a protocol for differentialmore » {sup 35}S-radiolabeling of HBB complexes in vivo and used it to examine the HBB complex assembly process. He has identified proteins required for M-ring assembly or stabilization and for the possible initiation of rod assembly. The rod is not stable until the P ring is assembled onto it. The monomers of the P and L rings are exported independent of flagellar assembly. These radiolabeling experiments have also enabled me to identify several new component proteins of the HBB complex.« less

Authors:
Publication Date:
Research Org.:
Yale Univ., New Haven, CT (USA)
OSTI Identifier:
5526781
Alternate Identifier(s):
OSTI ID: 5526781
Resource Type:
Miscellaneous
Resource Relation:
Other Information: Thesis (Ph. D.)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; PROTEINS; MOLECULAR STRUCTURE; SALMONELLA TYPHIMURIUM; MOLECULAR BIOLOGY; AMINO ACID SEQUENCE; CHEMICAL COMPOSITION; ELECTROPHORESIS; GENE REGULATION; GENES; SULFUR 35; TRACER TECHNIQUES; BACTERIA; BETA DECAY RADIOISOTOPES; BETA-MINUS DECAY RADIOISOTOPES; DAYS LIVING RADIOISOTOPES; EVEN-ODD NUCLEI; ISOTOPE APPLICATIONS; ISOTOPES; LIGHT NUCLEI; MICROORGANISMS; NUCLEI; ORGANIC COMPOUNDS; RADIOISOTOPES; SALMONELLA; SULFUR ISOTOPES 550201* -- Biochemistry-- Tracer Techniques; 550701 -- Microbiology-- Tracer Techniques

Citation Formats

Jones, C.J.. Structure and assembly of the flagellar hook-basal body complex of Salmonella typhimurium. United States: N. p., 1989. Web.
Jones, C.J.. Structure and assembly of the flagellar hook-basal body complex of Salmonella typhimurium. United States.
Jones, C.J.. Sun . "Structure and assembly of the flagellar hook-basal body complex of Salmonella typhimurium". United States. doi:.
@article{osti_5526781,
title = {Structure and assembly of the flagellar hook-basal body complex of Salmonella typhimurium},
author = {Jones, C.J.},
abstractNote = {The hook-basal body (HBB) complex is a multi-component structure which comprises a significant part of the bacterial flagellar motor. Electrophoretic mobility shifts of HBB complex component proteins from four non-flagellate mutants have enabled the author to assign each protein as being the product of the gene defective in each of the respective strains. The author has purified and characterized HBB complexes lacking either the L ring or both the P and L rings, and concluded that the 27-kDa basal-body protein is the major component of the L ring, and that the 38-kDa basal-body protein is the major component of the P ring. He has sequenced the genes encoding the subunit proteins of the M, P, and L rings of the basal body, and have examined both the gene and deduced amino acid sequences for clues regarding the regulation of these genes and the structure of their products. By quantitating the amount of {sup 35}S incorporated into the component protein vivo and correcting for the amount of contained in each protein (as deduced from gene sequencing data), he has determined the relative stoichiometries of most of the known component proteins of the HBB complex. He has developed a protocol for differential {sup 35}S-radiolabeling of HBB complexes in vivo and used it to examine the HBB complex assembly process. He has identified proteins required for M-ring assembly or stabilization and for the possible initiation of rod assembly. The rod is not stable until the P ring is assembled onto it. The monomers of the P and L rings are exported independent of flagellar assembly. These radiolabeling experiments have also enabled me to identify several new component proteins of the HBB complex.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Sun Jan 01 00:00:00 EST 1989},
month = {Sun Jan 01 00:00:00 EST 1989}
}

Miscellaneous:
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