The two-step lysis system of pneumococcal bacteriophage EJ-1 is functional in gram-negative bacteria: triggering of the major pneumococcal autolysin in Escherichia coli.
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Characterization and determination of holin protein of Streptococcus suis bacteriophage SMP in heterologous hostFull-length structure of the major autolysin LytAPurification and biochemical characterization of the lambda holin.The R-type pyocin of Pseudomonas aeruginosa is related to P2 phage, and the F-type is related to lambda phage.Identification and characterization of a lysis module present in a large proportion of bacteriophages infecting Streptococcus thermophilus.Reconstitution of holin activity with a synthetic peptide containing the 1-32 sequence region of EJh, the EJ-1 phage holin.Controlled autolysis facilitates the polyhydroxyalkanoate recovery in Pseudomonas putida KT2440.Purification and polar localization of pneumococcal LytB, a putative endo-beta-N-acetylglucosaminidase: the chain-dispersing murein hydrolase.Functional analysis of the two-gene lysis system of the pneumococcal phage Cp-1 in homologous and heterologous host cells.Mycobacteriophage D29 holin C-terminal region functionally assists in holin aggregation and bacterial cell death.Recent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage.Inducible cell lysis systems in microbial production of bio-based chemicals.Requirement of autolytic activity for bacteriocin-induced lysisThe N-terminal region of the Oenococcus oeni bacteriophage fOg44 lysin behaves as a bona fide signal peptide in Escherichia coli and as a cis-inhibitory element, preventing lytic activity on oenococcal cellsEvidence for a holin-like protein gene fully embedded out of frame in the endolysin gene of Staphylococcus aureus bacteriophage 187.Analysis of the complete nucleotide sequence and functional organization of the genome of Streptococcus pneumoniae bacteriophage Cp-1The autolysin LytA contributes to efficient bacteriophage progeny release in Streptococcus pneumoniaeExport of the pneumococcal phage SV1 lysin requires choline-containing teichoic acids and is holin-independent.The molecular characterization of the first autolytic lysozyme of Streptococcus pneumoniae reveals evolutionary mobile domains.
P2860
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P2860
The two-step lysis system of pneumococcal bacteriophage EJ-1 is functional in gram-negative bacteria: triggering of the major pneumococcal autolysin in Escherichia coli.
description
1996 nî lūn-bûn
@nan
1996 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
The two-step lysis system of p ...... autolysin in Escherichia coli.
@ast
The two-step lysis system of p ...... autolysin in Escherichia coli.
@en
The two-step lysis system of p ...... autolysin in Escherichia coli.
@nl
type
label
The two-step lysis system of p ...... autolysin in Escherichia coli.
@ast
The two-step lysis system of p ...... autolysin in Escherichia coli.
@en
The two-step lysis system of p ...... autolysin in Escherichia coli.
@nl
prefLabel
The two-step lysis system of p ...... autolysin in Escherichia coli.
@ast
The two-step lysis system of p ...... autolysin in Escherichia coli.
@en
The two-step lysis system of p ...... autolysin in Escherichia coli.
@nl
P2093
P921
P1476
The two-step lysis system of p ...... autolysin in Escherichia coli.
@en
P2093
P304
P356
10.1046/J.1365-2958.1996.399929.X
P407
P577
1996-02-01T00:00:00Z