Single stranded binding protein: Difference between revisions
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Phe-60 is an important DNA binding site. It has been shown to be the site for cross-linking. | Phe-60 is an important DNA binding site. It has been shown to be the site for cross-linking. | ||
Tryptophan and Lysine residues are important in binding as well. “Treatments resulting in | |||
modification of arginine, cysteine, or tyrosine residues had no effect on binding of SSB to | modification of arginine, cysteine, or tyrosine residues had no effect on binding of SSB to | ||
DNA, whereas modification of either lysine residues (with acetic anhydride) or tryptophan | |||
residues (with N-bromosuccinimide) led to complete loss of binding activity” ( Meyer, 348). | residues (with N-bromosuccinimide) led to complete loss of binding activity” ( Meyer, 348). | ||
The two tryptophan residues involved in DNA binding are Try-40 and Try-54, which was | The two tryptophan residues involved in DNA binding are Try-40 and Try-54, which was | ||
determined by mutagenesis. One more binding site was determined by site-specific mutagenesis. | determined by mutagenesis. One more binding site was determined by site-specific mutagenesis. | ||
When His-55 is substituted with Leu it decreases binding affinity. All of these residues | |||
are found in a hydrophobic region, which is suitable for nucleotide base interactions. | are found in a hydrophobic region, which is suitable for nucleotide base interactions. | ||
==SSB-Protein Interactions== | ==SSB-Protein Interactions== | ||
