Acg Atg Cat Cat Gtt Ttt Ttt Ttt Ttt Ttt Ttt Tcg Cga Acc Cta Ttt Agg Gtt Cgc
نویسندگان
چکیده
Dna2 is a nuclease/helicase with proposed roles in DNA replication, double-strand break repair and telomere maintenance. For each role Dna2 is proposed to process DNA substrates with a 50-flap. To date, however, Dna2 has not revealed a preference for binding or cleavage of flaps over single-stranded DNA. Using DNA binding competition assays we found that Dna2 has substrate structure specificity. The nuclease displayed a strong preference for binding substrates with a 50-flap or some variations of flap structure. Further analysis revealed that Dna2 recognized and bound both the single-stranded flap and portions of the duplex region immediately downstream of the flap. A model is proposed in which Dna2 first binds to a flap base, and then the flap threads through the protein with periodic cleavage, to a terminal flap length of 5 nt. This resembles the mechanism of flap endonuclease 1, consistent with cooperation of these two proteins in flap processing.
منابع مشابه
Nucleotide sequence of the gtfA gene from S. mutans GS-5.
5' AAGCTTCCAC TACCTTGCCA CCCGCAATAA GAACGATTAC TTCTCCCTCG CCTT 54 Kec Pro tie Thr Asn 141 CTACCA CCTAAAGATC TCCCTCTTAT TTTTAGOTTG AACTCGTATA AACCAAAATT AATTACACCA GATAAA ATG CCA ATT ACA AAT -35 -10 BBS fut Lys ThT Hec Leu Il« Thr Tyr Ala Aap Ser Leu Gly Lye Asa Leu Lys Glu Leu Asn Glu A«n H e Glu Agn Tyr AAA ACA ATG TTC ATT ACT TAC GCA CAC ACT TTC OGT AAA AAT TTG AAA CAA TTG AAT GAA AAT ATT GAG...
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