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| - Interactions between Coat and Scaffolding Proteins of Phage P22 Are Altered inVitro by Amino Acid Substitutions in Coat Protein That Cause a Cold-SensitivePhenotype
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| - Cold-sensitive mutations in phage P22 coat protein cause theaccumulation of precursor capsidsin cells growing at the nonpermissive temperature (16 °C). Theassembly of coat proteins which carrythe substitutions threonine at position 10 to isoluecine (T10I),arginine at position 101 to cysteine (R101C),or asparagine at position 414 to serine (N414S) which causecold-sensitivity has been investigated. Allthree proteins were found to fold into a monomeric species. Coatproteins carrying the amino acidsubstitutions T10I and R101C were not able to interact with scaffoldingprotein appropriately to initiateassembly in vitro while coat protein carrying thesubstitution N414S was able to assemble; however,capsids formed of this protein had an increased affinity forscaffolding protein. These amino acidsubstitutions define two regions in coat protein that are essential forthe interaction of coat protein withscaffolding protein at different stages in capsidmaturation.
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