TAILIEUCHUNG - Báo cáo khoa học: Integrase of Mason–Pfizer monkey virus

The gene encoding an integrase of Mason–Pfizer monkey virus (M-PMV) is located at the 3¢-end of the pol open reading frame. The M-PMV integ-rase has not been previously isolated and characterized. We have now cloned, expressed, isolated, and characterized M-PMV integrase and com-pared its activities and primary structure with those of HIV-1 and other retroviral integrases. M-PMV integrase prefers untranslated 3¢-region-derived long-terminal repeat sequences in both the 3¢-processing and the strand transfer activity assays. While the 3¢-processing reaction catalyzed by M-PMV integrase was significantly increased in the presence of Mn2+ and Co 2+ and was readily detectable in the presence of Mg 2+ and Ni 2+ cations, the strand transfer activity was strictly dependent. | ềFEBS Journal Integrase of Mason-Pfizer monkey virus lan Qnácal1 2 TdanaL 1 rztiXflx1 2 Cit d lQnnrw 01 2 l on RhcqoPtoK i1 T - mác Riiml1 JdH Ollaocl ZUclIck Ixiejcik Vela Jcliuova Ivan nOocHUciy lOlllao Rumi Jerry Alexandratos3 Alla Gustchina3 and Iva Pichova1 1 Institute of Organic Chemistry and Biochemistry Academy of Sciences of the Czech Republic Prague Czech Republic 2 Institute of Molecular Genetics and Center for Integrated Genomics Academy of Sciences of the Czech Republic Prague Czech Republic 3 Macromolecular Crystallography Laboratory NationalCancer Institute Frederick MD USA Keywords integrase Mason-Pfizer monkey virus HIV-1 specificity structure Correspondence I. Pichova Institute of Organic Chemistry and Biochemistry Academy of Sciences of the Czech Republic Flemingovo n. 2 166 10 Prague 6 Czech Republic Fax 42 02 20183556 Tel 42 02 20183251 E-mail Received 21 July 2004 revised 21 September 2004 accepted 22 September 2004 doi The gene encoding an integrase of Mason-Pfizer monkey virus M-PMV is located at the 3 -end of the pol open reading frame. The M-PMV integrase has not been previously isolated and characterized. We have now cloned expressed isolated and characterized M-PMV integrase and compared its activities and primary structure with those of HIV-1 and other retroviral integrases. M-PMV integrase prefers untranslated 3 -region-derived long-terminal repeat sequences in both the 3 -processing and the strand transfer activity assays. While the 3 -processing reaction catalyzed by M-PMV integrase was significantly increased in the presence of Mn2 and Co2 and was readily detectable in the presence of Mg2 and Ni2 cations the strand transfer activity was strictly dependent only on Mn2 . M-PMV integrase displays more relaxed substrate specificity than HIV-1 integrase catalyzing the cleavage and the strand transfer of M-PMV and HIV-1 long-terminal repeat-derived substrates with similar .

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