A variant protein from phi29 replication gene, gene 1, did not form homo-polymer due to a single amino acid substitution near the carboxyl terminus.
For study of the self-association of the product of psi29 gene 1, one variant which has a substitution at the 71(st) amino acid was used. By glycerol gradient sedimentation, the product of wild-type gene 1 existed both as large aggregate and oligomer, whereas the variant was detected as a single peak of monomer size. According to experiments using His-tagged proteins and Ni-NTA magnetic beads, the variant made only a little self-associated complex. From these results, a site essential for self-association was suggested to exist close to the carboxyl terminus of the product of psi29 gene 1.
Hashiyama
Kazuya
K
Department of Genetics, Life Science Institute, Sophia University, Tokyo, Japan.
Takeuchi
Ari
A
Makino
Osamu
O
D019943:Amino Acid Substitution; D017103:Bacillus Phages / Q000235:genetics* / Q000378:metabolism*; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics*
D014764:Viral Proteins; C040784:terminal protein, Bacillus phage phi29