First Evidence of a Functional Interaction between DNA Quadruplexes and Poly(ADP-ribose) Polymerase-1
Author(s) -
В А Солдатенков,
Alexandre A. Vetcher,
Tetyana Duka,
Sylvain Ladame
Publication year - 2008
Publication title -
acs chemical biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.899
H-Index - 111
eISSN - 1554-8937
pISSN - 1554-8929
DOI - 10.1021/cb700234f
Subject(s) - telomere , g quadruplex , polymerase , dna , poly adp ribose polymerase , transcription (linguistics) , biochemistry , microbiology and biotechnology , biology , in vitro , chemistry , ribose , enzyme , linguistics , philosophy
We discovered that the abundant human nuclear protein poly(ADP-ribose) polymerase-1 (hPARP-1) binds to intramolecular DNA quadruplexes in vitro with high affinity and with a stoichiometry of two proteins for one quadruplex. Using an enzymatic assay, we have shown that hPARP-1 gets catalytically activated upon binding to G-quadruplexes localized at the c-kit promoter and human telomere regions. This is the first example of a truly functional quadruplex-protein interaction, which has possible implications in understanding hPARP-1 mediated mechanisms of transcription regulation and telomere end protection.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom