FN Archimer Export Format PT J TI Novel inhibition of archaeal family-D DNA polymerase by uracil BT AF RICHARDSON, Tomas T. GILROY, Louise ISHINO, Yoshizumi CONNOLLY, Bernard A. HENNEKE, Ghislaine AS 1:1;2:1;3:2;4:1;5:3,4,5; FF 1:;2:;3:;4:;5:PDG-REM-EEP-LMEE; C1 Newcastle Univ, Inst Cell & Mol Biosci ICaMB, Newcastle Upon Tyne NE2 4HH, Tyne & Wear, England. Kyushu Univ, Grad Sch Bioresourse & Bioenvironm Sci, Dept Biosci & Biotechnol, Fukuoka 8128581, Japan. IFREMER, Ctr Brest, UMR 6197, LM2E, F-29280 Plouzane, France. CNRS, LM2E, UMR 6197, F-29280 Plouzane, France. Univ Brest, UEB, LM2E, UMR 6197, F-29280 Plouzane, France. C2 UNIV NEWCASTLE, UK UNIV KYUSHU, JAPAN IFREMER, FRANCE CNRS, FRANCE UBO, FRANCE SI BREST SE PDG-REM-EEP-LMEE IN WOS Ifremer jusqu'en 2018 copubli-france copubli-europe copubli-univ-france copubli-int-hors-europe IF 8.808 TC 13 UR https://archimer.ifremer.fr/doc/00138/24975/23070.pdf LA English DT Article AB Archaeal family-D DNA polymerase is inhibited by the presence of uracil in DNA template strands. When the enzyme encounters uracil, following three parameters change: DNA binding increases roughly 2-fold, the rate of polymerization slows by a factor of similar to 5 and 3'-5' proof-reading exonuclease activity is stimulated by a factor of similar to 2. Together these changes result in a significant decrease in polymerization activity and a reduction in net DNA synthesis. Pol D appears to interact with template strand uracil irrespective of its distance ahead of the replication fork. Polymerization does not stop at a defined location relative to uracil, rather a general decrease in DNA synthesis is observed. 'Trans' inhibition, the slowing of Pol D by uracil on a DNA strand not being replicated is also observed. It is proposed that Pol D is able to interact with uracil by looping out the single-stranded template, allowing simultaneous contact of both the base and the primer-template junction to give a polymerase-DNA complex with diminished extension ability. PY 2013 PD APR SO Nucleic Acids Research SN 0305-1048 PU Oxford Univ Press VL 41 IS 7 UT 000318167900037 BP 4207 EP 4218 DI 10.1093/nar/gkt083 ID 24975 ER EF