Single-stranded telomere-binding protein employs a dual rheostat for binding affinity and specificity that drives function.

ABSTRACT: ssDNA, which is involved in numerous aspects of chromosome biology, is managed by a suite of proteins with tailored activities. The majority of these proteins bind ssDNA indiscriminately, exhibiting little apparent sequence preference. However, there are several notable exceptions, including the Saccharomyces cerevisiae Cdc13 protein, which is vital for yeast telomere maintenance. Cdc13 is one of the tightest known binders of ssDNA and is specific for G-rich telomeric sequences. To investigate how these two different biochemical features, affinity and specificity, contribute to function, we created an unbiased panel of alanine mutations across the Cdc13 DNA-binding interface, including several aromatic amino acids that play critical roles in binding activity. A subset of mutant prot

SUBMITTER: Glustrom LW 

PROVIDER: S-EPMC6187146 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature