Purification and characterization of the flagellar hook-basal body complex of Salmonella typhimurium.

Abstract:

:The hook-basal body complex of Salmonella typhimurium, a major component of its flagellar apparatus, was subjected to detailed analysis by electron microscopy and gel electrophoresis. The study was facilitated by the development of an improved protocol for isolation of the complexes in high yield and purity. Nine proteins were identified with the structure. These proteins had apparent molecular weights of 65,000 (65K), 60K, 42K, 38K, 32K, 30K, 27K, 16K, and 14K. Small but reproducible shifts in the apparent molecular weights of specific proteins from conditionally nonflagellate mutants indicated the following gene-polypeptide correspondences: flaFV, 42K; flaFVI, 32K; flaFVII, 30K; flaFIX, 38K; flaAII.1, 65K. Several new morphological features of hook-basal body complexes were recognized, including a clawlike structure on the cytoplasm-proximal M ring and additional material at the cytoplasmic face of the M ring. Based on this study and the work of others, we suggest that the morphological features of the hook-basal body complex correspond to the following proteins: hook-filament junction, 60K; hook, 42K; rod, 30K and 32K; L ring and outer cylinder wall, 27K; P ring, 38K; S ring, unknown; M ring 65K.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Aizawa SI,Dean GE,Jones CJ,Macnab RM,Yamaguchi S

doi

10.1128/JB.161.3.836-849.1985

subject

Has Abstract

pub_date

1985-03-01 00:00:00

pages

836-49

issue

3

eissn

0021-9193

issn

1098-5530

journal_volume

161

pub_type

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