A peptidoglycan hydrolase motif within the mycobacteriophage TM4 tape measure protein promotes efficient infection of stationary phase cells.

A peptidoglycan hydrolase motif within the mycobacteriophage TM4 tape measure protein promotes efficient infection of stationary phase cells. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

A peptidoglycan hydrolase motif within the mycobacteriophage TM4 tape measure protein promotes efficient infection of stationary phase cells. Abstract Text:

Mariana Piuri,Graham F Hatfull,

The predominant morphotype of mycobacteriophage virions has a DNA-containing capsid attached to a long flexible non-contractile tail, features characteristic of the Siphoviridae. Within these phage genomes the tape measure protein (tmp) gene can be readily identified due to the well-established relationship between the length of the gene and the length of the phage tail--because these phages typically have long tails, the tmp gene is usually the largest gene in the genome. Many of these mycobacteriophage Tmp's contain small motifs with sequence similarity to host proteins. One of these motifs (motif 1) corresponds to the Rpf proteins that have lysozyme activity and function to stimulate growth of dormant bacteria, while the others (motifs 2 and 3) are related to proteins of unknown function, although some of the related proteins of the host are predicted to be involved in cell wall catabolism. We show here that motif 3-containing proteins have peptidoglycan-hydrolysing activity and that while this activity is not required for phage viability, it facilitates efficient infection and DNA injection into stationary phase cells. Tmp's of mycobacteriophages may thus have acquired these motifs in order to avoid a selective disadvantage that results from changes in peptidoglycan in non-growing cells.

A peptidoglycan hydrolase motif within the mycobacteriophage TM4 tape measure protein promotes efficient infection of stationary phase cells. Publishing Authors By Initials

M Piuri,GF Hatfull,

For similar proteins: viral proteins research abstracts see: proteins: viral proteins research

PUBMED ID PMID:

MEDLINE DATE:

A peptidoglycan hydrolase motif within the mycobacteriophage TM4 tape measure protein promotes efficient infection of stationary phase cells. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Molecular microbiology

VOLUME: 62

Page Numbers: 1569-85

Journal Abbreviation:

ISSN: 0950-382X

DAY: 3

MONTH: Dec

YEAR: 2006

A peptidoglycan hydrolase motif within the mycobacteriophage TM4 tape measure protein promotes efficient infection of stationary phase cells. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8712028

A peptidoglycan hydrolase motif within the mycobacteriophage TM4 tape measure protein promotes efficient infection of stationary phase cells. Keywords Mesh Terms:

KEYWORDS: Viral Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: A peptidoglycan hydrolase motif within the mycobacteriophage TM4 tape measure protein promotes efficient infection of stationary phase cells. Information

Substance Name: N-Acetylmuramoyl-L-alanine Amidase

Registry Number: EC 3.5.1.28

Grant and Affiliation Information for A peptidoglycan hydrolase motif within the mycobacteriophage TM4 tape measure protein promotes efficient infection of stationary phase cells.

AFFILIATION: Pittsburgh Bacteriophage Institute and Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.

Country: England

AGENCY: United States NIAID

GRANT: AI28927

ACRONYM: AI

MEDLINETA: Mol Microbiol

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

A peptidoglycan hydrolase motif within the mycobacteriophage TM4 tape measure protein promotes efficient infection of stationary phase cells Related Publications

• A peptidoglycan hydrolase motif within the mycobacteriophage TM4 tape measure protein promotes efficient infection of stationary phase cells.
• Comparative genomic analysis of mycobacteriophage Tweety: evolutionary insights and construction of compatible site-specific integration vectors for mycobacteria.
• Control of phage Bxb1 excision by a novel recombination directionality factor.
• Genomic characterization of mycobacteriophage giles: evidence for phage acquisition of host DNA by illegitimate recombination.
• Growth of Mycobacterium tuberculosis biofilms containing free mycolic acids and harbouring drug-tolerant bacteria.
• Mycobacterial recombineering.
• Recombineering in Mycobacterium tuberculosis.
• Recombineering mycobacteria and their phages.
• The assay of methyl salicylate ointments.
• The role of iron in Mycobacterium smegmatis biofilm formation: the exochelin siderophore is essential in limiting iron conditions for biofilm formation but not for planktonic growth.
• Two-step site selection for serine-integrase-mediated excision: DNA-directed integrase conformation and central dinucleotide proofreading.