Replication factor C recognizes 5'-phosphate ends of telomeres

Biochemical and Biophysical Research Communications
F UchiumiS i Tanuma

Abstract

Telomere structure is suggested to be important for chromosome and cell integrity and thereby for cell senescence and immortality. In a search for cDNA encoding proteins that bind specifically to telomere repeat sequences, we used random primer-labeled telomere probes to screen a lambda gt11 Jurkat cDNA library. The clone obtained encodes the central region of the large subunit of replication factor C (RFC), a known activator of DNA polymerase delta. Electrophoretic mobility shift analyses of the binding ability of RFC-glutathione S-transferase (GST) fusion protein to telomere probes revealed that RFC recognizes preferentially 5'-phosphoryl (P) groups but not 3'-hydroxyl (OH) groups at the ends of double-stranded telomere repeats. This structure-specific binding of RFC is supported by the observations that it binds to 3'-OH/5'-P ends in telomere repeats produced by DNase gamma, but not to those produced by 3'-P/5'-OH ends for DNase alpha. These findings suggest a novel function for RFC in telomere stability or turnover.

Citations

Jun 16, 2005·Bioinformatics·Purvesh KhatriSorin Draghici
Sep 2, 2011·The Journal of Infectious Diseases·Mark LoebMathieu Lemire
Dec 17, 2008·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·Fumiaki UchiumiSei-ichi Tanuma
Sep 25, 2017·The Journal of Gene Medicine·Yu-Huang LiaoZe-Fang Ren
May 18, 1999·Biochemical and Biophysical Research Communications·F UchiumiS i Tanuma
Sep 11, 2004·Biochemical and Biophysical Research Communications·Fumiaki UchiumiSei-ichi Tanuma

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