Browsing Prof. Pradeep Parrack by Title
Now showing items 1-9 of 9
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Cyclic AMP-dependent functional forms of cyclic AMP receptor protein from Vibrio cholerae
(ELSEVIER SCIENCE INC, 2006-03-01)The cyclic AMP receptor protein (CRP) from Escherichia coli, involved in the transcriptional regulation of a number of genes and operons, works by binding to specific sites upstream of promoters. CRP also binds cyclic AMP ... -
Direct CIII-HflB interaction is responsible for the inhibition of the HflB (FtsH)-mediated proteolysis of Escherichia coli sigma(32) by lambda CIII
(WILEY-BLACKWELL, 2008-10)The CIII protein of bacteriophage lambda exhibits antiproteolytic activity against the ubiquitous metalloprotease HflB (FtsH) of Escherichia coli, thereby stabilizing the lambda CII protein and promoting lysogenic development ... -
E. coli HflX interacts with 50S ribosomal subunits in presence of nucleotides
(ACADEMIC PRESS INC ELSEVIER SCIENCE, 2009-02-06)HflX is a GTP binding protein of unknown function. Based on the presence of the hflX gene in hflA operon, HflX was believed to be involved in the lytic-lysogenic decision during phage infection in Escherichia coli. We find ... -
HflD, an Escherichia coli protein involved in the lambda lysis-lysogeny switch, impairs transcription activation by lambda CII
(ELSEVIER SCIENCE, 2010-01-15)The CII protein of bacteriophage lambda is the key regulator for the lytic–lysogenic choice of the viral lifecycle. An unstable homotetrameric transcription activator of the three phage promoters pE, pI and paQ, λCII is ... -
Probing the antiprotease activity of lambda CIII, an inhibitor of the Escherichia coli metalloprotease HflB (FtsH)
(AMER SOC MICROBIOLOGY, 2007-11)The CIII protein encoded by the temperate coliphage lambda acts as an inhibitor of the ubiquitous Escherichia coli metalloprotease HflB (FtsH). This inhibition results in the stabilization of transcription factor lambda ... -
Properties of HflX, an Enigmatic Protein from Escherichia coli
(AMER SOC MICROBIOLOGY, 2009-04-01)The Escherichia coli gene hflX was first identified as part of the hflA operon, mutations in which led to an increased frequency of lysogenization upon infection of the bacterium by the temperate coliphage lambda. Independent ... -
Role of C-terminal residues in oligomerization and stability of λ CII: Implications for lysis-lysogeny decision of the phage
(ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD, 2005-01-14)A crucial element in the lysis-lysogeny decision of the temperate coliphage lambda is the phage protein CII, which has several interesting properties. It promotes lysogeny through activation of three phage promoters p(E), ... -
Specific hydrophobic residues in the alpha 4 helix of lambda CII are crucial for maintaining its tetrameric structure and directing the lysogenic choice
(SOC GENERAL MICROBIOLOGY, 2010-01)The CII protein of the temperate bacteriophage l is the decision-making factor that determines the viral lytic/lysogenic choice. It is a homotetrameric transcription activator that recognizes and binds specific direct ... -
Studies on Escherichia coli HflKC suggest the presence of an unidentified lambda factor that influences the lysis-lysogeny switch
(BIOMED CENTRAL, 2011-02-17)Background: The lysis-lysogeny decision in the temperate coliphage γ is influenced by a number of phage proteins (CII and CIII) as well as host factors, viz. Escherichia coli HflB, HflKC and HflD. Prominent among these are ...