The mycobacteriophage Ms6 encodes a chaperone-like protein involved in the endolysin delivery to the peptidoglycan.
作者： Maria João Catalão , Filipa Gil , José Moniz-Pereira , Madalena Pimentel
DOI: 10.1111/J.1365-2958.2010.07239.X
关键词:
摘要: Like most double-stranded (ds) DNA phages, mycobacteriophage Ms6 uses the holin-endolysin system to achieve lysis of its host. In addition endolysin (lysA) and holin (hol) genes, encodes three accessory proteins. this study we investigated function Gp1, which is encoded by gp1 gene that lies immediately upstream lysA. Escherichia coli was observed after coexpression LysA Gp1 in absence holin. does not belong class proteins, provide evidence it shares several characteristics with molecular chaperones. We show interacts LysA, interaction necessary for delivery target. addition, PhoA fusions showed that, Mycobacterium smegmatis, exported extracytoplasmic environment presence Gp1. also efficient M. smegmatis lysis, as deletion results host defects. propose murein layer assisted a chaperone-like protein, holin-independent manner.
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