Single stranded binding protein: Difference between revisions

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Refayat Ahsen, Rachel Craig, Alexander Berchansky, Michal Harel

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 ====Interactions Between ''E. coli'' SSB and other Proteins====
-Most of the molecule loses flexibility after ssDNA binding.  However, three <scene name='56/566528/Phe_residues/1'>phenylalanine residues</scene> (Phe147, Phe171, Phe177) in the COOH terminal domain remain flexible, even after DNA binding, suggesting that the COOH terminus has something to do with protein binding <ref>PMID:2087220</ref>.  An experiment where Phe177 was changed to Cys resulted in a protein that could not replicate DNA. This replication defect stemming from the lost phenylalanine residue was likely a result of the inability of the altered C-terminal region to bind other proteins necessary for replication <ref>PMID:2453719</ref>.
+Most of the molecule loses flexibility after ssDNA binding.  However, three phenylalanine residues (Phe147, Phe171, Phe177) in the COOH terminal domain remain flexible, even after DNA binding, suggesting that the COOH terminus has something to do with protein binding <ref>PMID:2087220</ref>.  An experiment where Phe177 was changed to Cys resulted in a protein that could not replicate DNA. This replication defect stemming from the lost phenylalanine residue was likely a result of the inability of the altered C-terminal region to bind other proteins necessary for replication <ref>PMID:2453719</ref>.
 <scene name='56/566528/Gly_15/2'>Gly15</scene> is believed to play an important role in binding the RecA protein.  SSB will interact with the protein RecA to enable recombination, because RecA will recognize SSB and replace it on the strand. In DNA repair, SSB will bind to the damaged strand to protect it. And eventually it will attract repair enzymes which will replace SSB and begin repair mechanisms.  Mutations in <scene name='56/566528/Gly_15/2'>Gly15</scene> have been shown to have extreme effects on recombinational repair.  SSB is also thought to bind with exonuclease I, DNA polymerase II, and a protein n, which is a part of the primosome complex and used to help synthesize RNA primers for the lagging strand <ref>PMID: 2087220</ref>.