منابع مشابه
The Holin protein of bacteriophage PRD1 forms a pore for small-molecule and endolysin translocation.
PRD1 is a bacteriophage with an icosahedral outer protein layer surrounding the viral membrane, which encloses the linear double-stranded DNA genome. PRD1 infects gram-negative cells harboring a conjugative IncP plasmid. Here we studied the lytic functions of PRD1. Using infected cells and plasmid-borne lysis genes, we demonstrated that a two-component lysis system (holin-endolysin) operates to...
متن کاملTranslocation and specific cleavage of bacteriophage T7 DNA in vivo by EcoKI.
Infection of Escherichia coli containing the type I restriction enzyme EcoKI by bacteriophage T7 0.3 mutants leads to restriction during the late stages of genome entry and during DNA replication. Patterns of cleavage in vivo suggest that some cutting occurs near the midpoint of two recognition sites, consistent with the idea that EcoKI translocates DNA bidirectionally through itself and cuts w...
متن کاملTranslocation of nicked but not gapped DNA by the packaging motor of bacteriophage phi29.
The biomolecular mechanism that the double-stranded DNA viruses employ to insert and package their genomic DNA into a preformed procapsid is still elusive. To better characterize this process, we investigated packaging of bacteriophage phi29 DNA with structural alterations. phi29 DNA was modified in vitro by nicking at random sites with DNase I, or at specific sites with nicking enzyme N.BbvC I...
متن کاملBacteriophage Xp10 anti-termination factor p7 induces forward translocation by host RNA polymerase
Regulation of transcription elongation is based on response of RNA polymerase (RNAP) to various pause signals and is modulated by various accessory factors. Here we report that a 7 kDa protein p7 encoded by bacteriophage Xp10 acts as an elongation processivity factor of RNAP of host bacterium Xanthomonas oryzae, a major rice pathogen. Our data suggest that p7 stabilizes the upstream DNA duplex ...
متن کاملInositol phospholipids: Translocation, translocation, translocation …
The pleckstrin homology (PH) domains of a number of proteins have been found to interact in vitro with inositol phospholipids; recent experiments show that these interactions may be important in directing protein translocation to specific parts of the cell following stimulus-induced lipid breakdown or synthesis.
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ژورنال
عنوان ژورنال: FEMS Immunology & Medical Microbiology
سال: 2006
ISSN: 0928-8244,1574-695X
DOI: 10.1111/j.1574-695x.2006.00044.x