Bacteriophage ms2 l protein: genetic and biochemical characterization

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dc.contributor.advisor Young , Ryland F , en_US
dc.contributor.committeeMember Golden , James en_US
dc.creator McIntosh , Brenley Kathleen en_US 2010 -01 -15T00 :12 :48Z 2014 -02 -19T19 :32 :35Z 2010 -01 -15T00 :12 :48Z 2014 -02 -19T19 :32 :35Z 2008 -05 en_US 2009 -05 -15 en_US
dc.identifier.uri http : / /hdl .handle .net /1969 .1 /ETD -TAMU -2764
dc.description.abstract In order to release progeny , bacteriophages must lyse the host cell by compromising the peptidoglycan layer . There are two known strategies of lysis : the holin -endolysin system and single gene lysis (SGL ) , which are dependent on the genome size . Large phages encode multiple proteins , including a holin and endolysin , for lysis . In contrast , small ssRNA phages (Leviviridae and Alloleviviridae ) and ssDNA phages (Microviridae ) do not encode a muralytic enzyme and accomplish lysis with a single gene . The cellular target of the lysis gene E from the prototypic microvirus , ?X174 , and A2 from the prototypic allolevivirus , Q ? , has been elucidated . In both cases , these proteins were demonstrated to inhibit specific enzymes within the peptidoglycan biosynthetic pathway and infected cells lyse as a result of septal catastrophes . The prototype Levivirus MS2 encodes L , a 75 aa polypeptide that effects lysis without inhibiting murein synthesis . The purpose of the work described in this dissertation was to characterize MS2 L using genetic and biochemical strategies . Using a genetic approach , PcnB was shown to be important to the entry of the MS2 RNA into the cytoplasm . L accumulation during infection was quantified by comparison to purified , oligohistidine -tagged L . Biochemical experiments demonstrated the L protein behaved as a periplasmic , membrane -associated protein . The morphologies of cells undergoing L -mediated lysis are significantly different from cells lysing due to A2 expression , since L -lysing cells do not show septally localized membrane protrusions . en_US
dc.format.medium electronic en_US
dc.format.mimetype application /pdf en_US
dc.language.iso en _US en_US
dc.subject Bacteriophage en_US
dc.title Bacteriophage ms2 l protein : genetic and biochemical characterization en_US
dc.type Book en
dc.type.genre Electronic Dissertation en_US
dc.type.material text en_US
dc.format.digitalOrigin born digital en_US


Bacteriophage ms2 l protein: genetic and biochemical characterization. Available electronically from http : / /hdl .handle .net /1969 .1 /ETD -TAMU -2764 .

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