Single stranded binding protein: Difference between revisions
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SSB can form complexes with many other proteins. This trait can keep enzymes needed for damage repair, transcription, etc. near the ssDNA and it is thought that SSB can even help to stimulate these enzymes to carry out their jobs. When DNA binds SSB, most of the molecule loses flexibility. But three of the phenylalanines (147, 171, 177) in the COOH terminal domain remain flexible, even after DNA binding. It is believed that the COOH terminus has something to do with protein binding <ref>PMID: 2087220</ref>. | SSB can form complexes with many other proteins. This trait can keep enzymes needed for damage repair, transcription, etc. near the ssDNA and it is thought that SSB can even help to stimulate these enzymes to carry out their jobs. When DNA binds SSB, most of the molecule loses flexibility. But three of the phenylalanines (147, 171, 177) in the COOH terminal domain remain flexible, even after DNA binding. It is believed that the COOH terminus has something to do with protein binding <ref>PMID: 2087220</ref>. | ||
One experiment in which Phe-177 was changed to Cys resulted in a protein that could not replicate DNA. This replication defect results from the inability of C-terminus to bind to other replication proteins <ref>PMID: 2453719</ref>. | |||
It is believed that Gly15 may play an important role in binding the RecA protein. Mutations in Gly15 have | It is believed that Gly15 may play an important role in binding the RecA protein. Mutations in Gly15 have | ||
extreme effects on recombinational repair. SSB has also been thought to bind with exonuclease I, DNA polymerase II, | extreme effects on recombinational repair. SSB has also been thought to bind with exonuclease I, DNA polymerase II, | ||
