Characterization of a flagellar sheath component, PF60, and its structural gene in marine Vibrio.

Characterization of a flagellar sheath component, PF60, and its structural gene in marine Vibrio. Research Abstract Details 

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Characterization of a flagellar sheath component, PF60, and its structural gene in marine Vibrio. Abstract Text:

M Furuno,K Sato,I Kawagishi,M Homma,

The Polar flagella (Pof) of Vibrio alginolyticus are surrounded by a membrane structure called a sheath. Five major proteins, whose molecular masses are 60, 47, 45, 44, and 18 kDa (named PF60, PF47, PF45, PF44, and PF18, respectively), have been detected in polar flagella. PF47 and PF45 have been identified as flagellins while the other proteins are thought to be sheath-associated ones. In this study, we isolated and partially characterized a major sheath protein, PF60. We found that PF60 can be solubilized by Triton X-100 treatment, but not by heat or acid treatment. After digestion with a peptidase, the N-terminal sequences of several fragments were determined and the N-terminus of intact PF60 seemed to be blocked. Through PCR in conjunction with oligonucleotide primers deduced from the peptide sequences, a DNA fragment of PF60 was amplified. A 4.5 kb HindIII restriction fragment was cloned by colony hybridization using the PCR fragment. Subsequent sequence analysis revealed three complete and one partial open reading frame (ORFs). The three ORFs, which exhibit sequence homology, correspond to PF60 (named pfsA), an amino acid transport ATP-binding protein, and an amino acid binding periplasmic protein. The single pfsA gene constitutes an operon and encodes a protein of 491 amino acids containing a putative signal peptide sequence at the N-terminal. A sequence database search revealed no homologous protein. However, PfsA seems to resemble lipoproteins in the N-terminal signal sequence and the biochemical data obtained in this study are consistent with that PfsA is a lipoprotein. The expression of the pfsA gene may be coordinately regulated with flagellar formation and similarly regulated to PF47 flagellin.

Characterization of a flagellar sheath component, PF60, and its structural gene in marine Vibrio. Publishing Authors By Initials

M Furuno,K Sato,I Kawagishi,M Homma,

For similar bacteria: gram-negative bacteria: gram-negative facultatively anaerobic rods: vibrionaceae: vibrio research abstracts see: bacteria: gram-negative bacteria: gram-negative facultatively anaerobic rods: vibrionaceae: vibrio research

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Characterization of a flagellar sheath component, PF60, and its structural gene in marine Vibrio. Journal Published:

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

Journal: Journal of biochemistry

VOLUME: 127

Page Numbers: 29-36

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jan

YEAR: 2000

Characterization of a flagellar sheath component, PF60, and its structural gene in marine Vibrio. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Characterization of a flagellar sheath component, PF60, and its structural gene in marine Vibrio. Keywords Mesh Terms:

KEYWORDS: Vibrio

MESH TERMS: genetics

Chemical & Substance for Abstract: Characterization of a flagellar sheath component, PF60, and its structural gene in marine Vibrio. Information

Substance Name: Flagellin

Registry Number: 12777-81-0

Grant and Affiliation Information for Characterization of a flagellar sheath component, PF60, and its structural gene in marine Vibrio.

AFFILIATION: Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan. g44416a@nucc.cc. nagoya-u.ac.jp

Country: JAPAN

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MEDLINETA: J Biochem

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ACCESSION NUMBER: AB032934

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