revisiting plus-strand dna synthesis in retroviruses and long terminal repeat retrotransposons dynamics of enzyme substrate interactions回顾正链dna合成在逆转录病毒和长末端重复反转位子活动动态酶底物的相互作用.pdfVIP

revisiting plus-strand dna synthesis in retroviruses and long terminal repeat retrotransposons dynamics of enzyme substrate interactions回顾正链dna合成在逆转录病毒和长末端重复反转位子活动动态酶底物的相互作用.pdf

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revisiting plus-strand dna synthesis in retroviruses and long terminal repeat retrotransposons dynamics of enzyme substrate interactions回顾正链dna合成在逆转录病毒和长末端重复反转位子活动动态酶底物的相互作用

Viruses 2009, 1, 657-677; doi:10.3390/v1030657 OPEN ACCESS viruses ISSN 1999-4915 /journal/viruses Review Revisiting Plus-Strand DNA Synthesis in Retroviruses and Long Terminal Repeat Retrotransposons: Dynamics of Enzyme: Substrate Interactions 1 2 3, Daniele Fabris , John P. Marino and Stuart F.J. Le Grice * 1 Department of Chemistry and Biochemistry, University of Maryland Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21228, USA 2 Center for Advanced Research in Biotechnology of the University of Maryland Biotechnology Institute and the National Institute of Standards and Technology, 9600 Gudelsky Drive, Rockville, MD 20850, USA 3 HIV Drug Resistance Program, NCI, National Institutes of Health, Frederick, MD 21702-1201, USA * Author to whom correspondence should be addressed; E-Mail: legrices@; Tel.: +1-301-846-5256; Fax: +1-301-846-6013. Received: 10 September 2009; in revised form: 28 October 2009 / Accepted: 4 November 2009 / Published: 4 November 2009 Abstract: Although polypurine tract (PPT)-primed initiation of plus-strand DNA synthesis in retroviruses and LTR-containing retrotransposons can be accurately duplicated, the molecular details underlying this concerted series of events remain largely unknown. Importantly, the PPT 3’ terminus must be accommodated by ribonuclease H (RNase H) and DNA polymerase catalytic centers situated at either terminus of the cognate reverse tra

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