Oligomerization of the bacteriophage lambda S protein in the inner membrane of Escherichia coli.

Abstract:

:Western blot (immunoblot) analysis of cell extracts from induced bacteriophage lambda lysogens probed with S-protein-specific antibody (raised against an S--beta-galactosidase fusion protein) demonstrated that the bacteriophage lambda S protein begins to appear 10 min after phage induction and is localized to the inner membrane at all times during the lytic cycle. Between 100 and 1,000 molecules of S protein per cell were present at the time of phage-induced lysis. Western blots of chemically cross-linked membranes from induced lysogens showed a ladder of bands at 18, 24, 32, and 42 kilodaltons (the S-protein monomer ran at 8 kilodaltons) that reacted with anti-S-protein antibody. Thus, the S protein appears to reside in the inner membrane as a multimer, and the molecular weights of the cross-linked species are consistent with those of S-protein homopolymers. Sodium dodecyl sulfate-resistant dimers were also detected when S protein was purified by immunoprecipitation.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Zagotta MT,Wilson DB

doi

10.1128/jb.172.2.912-921.1990

subject

Has Abstract

pub_date

1990-02-01 00:00:00

pages

912-21

issue

2

eissn

0021-9193

issn

1098-5530

journal_volume

172

pub_type

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