Genetic analysis of the T4 holin: timing and topology

The t protein of bacteriophage T4 shares with other holins the ability to cause the formation of a lethal membrane lesion which allows the phage endolysin to attack the peptidoglycan. Moreover, T, like other holins, acts in a saltatory manner at a precisely programmed time in the vegetative cycle. U...

Full description

Saved in:
Bibliographic Details
Published in:Gene 2001-03, Vol.265 (1-2), p.25-36
Main Authors: Ramanculov, E, Young, R
Format: Article
Language:English
Subjects:
Alkaline Phosphatase - genetics
Alkaline Phosphatase - metabolism
Alleles
Amino Acid Sequence
At protein
Bacteriolysis - genetics
Bacteriophage T4 - genetics
Bacteriophage T4 - growth & development
beta-Galactosidase - genetics
beta-Galactosidase - metabolism
endolysin
Lac Operon - genetics
Molecular Sequence Data
Mutation
peptidoglycans
Phage T4
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Sequence Deletion
Sequence Homology, Amino Acid
t gene
T protein
Time Factors
Viral Proteins - genetics
Viral Proteins - isolation & purification
Viral Proteins - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The t protein of bacteriophage T4 shares with other holins the ability to cause the formation of a lethal membrane lesion which allows the phage endolysin to attack the peptidoglycan. Moreover, T, like other holins, acts in a saltatory manner at a precisely programmed time in the vegetative cycle. Unlike other holins, however, T has the unique ability to postpone its lethal function in response to a secondary infection by a T-even phage during the vegetative cycle. A signal transduction system that responds to the secondary infection is thought to be encoded by some of the numerous r genes, defined by mutations that abolish this lysis-inhibition (LIN) response. The primary structure of T differs from two main structural patterns found in more than 30 orthologous groups of holins. Genetic approaches were taken to probe the t sequence for features involved in membrane localization, functional timing and LIN regulation. Gene fusion analysis indicates that T has a single TMD near the N-terminus, with the bulk of the protein residing in the periplasm. Mapping and phenotypic analysis of deletion and point mutations in t indicates that the periplasmic domain of T is the major determinant of the timing mechanism and is involved in the LIN response.
ISSN:0378-1119
DOI:10.1016/s0378-1119(01)00365-1