The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA

Article Abstract:

The structure-function relationship of telomeres was examined by combining the DNA binding protein RAP1 to telomeres and subjecting the resulting structure to X-ray crystallographic studies. RAP1 was found to contain two domains that bind the DNA in a tandem manner in recognition of a tandemly DNA sequence of 6-8 bp that is repeated in tandem. Binding specificity is effected by a structured linker and a long C-terminal tail which acts on the N-terminal tip of the recognition helix H1C of domain 1.

Yeast, Yeast (Food product), DNA binding proteins

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Civ1 (CAK in vivo), a novel Cdk-activating kinase

Article Abstract:

Cyclin-dependent protein kinases (Cdks) are essential elements in the regulation of cell division and gene expression. To be active, Cdks usually require the binding of a cyclin and phosphorylation by a Cdk-activating kinase (CAK). Civ1 (CAK in vivo) was identified in Saccharomyces cerevisiae. The sequence of Civ1 has the greatest similarity to that of the Cdks. However, Civ1 is different in that it is active as a monomer. Thus, it could be the founding member of a novel family of kinases.

Research, Analysis, Protein kinases, Phosphorylation

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An alternative pathway for yeast telomere maintenance rescues est1- senescence

Article Abstract:

Majority of Saccharomyces cerevisiae cells without the est1 gene die due to a continuous decline in the terminal G1-3T telomeric repeat. The minority population of yeast cells that survive were analyzed. The surviving est1- population was found to acquire and amplify subtelomeric elements by most or all telomeres. Thus, an alternative pathway for yeast telomere maintenance restores telomere function and keeps the yeast cells alive when the pathway for telomere replication is defective.

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