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Titolo:
KINETICS OF INTERACTION OF HIV REVERSE-TRANSCRIPTASE WITH PRIMER TEMPLATE
Autore:
DIVITA G; MULLER B; IMMENDORFER U; GAUTEL M; RITTINGER K; RESTLE T; GOODY RS;
Indirizzi:
MAX PLANCK INST MED RES,BIOPHYS ABT,JAHNSTR 29 W-6900 HEIDELBERG 1 GERMANY MAX PLANCK INST MED RES,BIOPHYS ABT,JAHNSTR 29 W-6900 HEIDELBERG 1 GERMANY EMBL W-6900 HEIDELBERG GERMANY
Titolo Testata:
Biochemistry
fascicolo: 31, volume: 32, anno: 1993,
pagine: 7966 - 7971
SICI:
0006-2960(1993)32:31<7966:KOIOHR>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; STEADY-STATE KINETICS; ESCHERICHIA-COLI; NONNUCLEOSIDE INHIBITORS; BINDING-SITE; EXPRESSION; REPLICATION; MECHANISM; PROCESSIVITY; DERIVATIVES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
G. Divita et al., "KINETICS OF INTERACTION OF HIV REVERSE-TRANSCRIPTASE WITH PRIMER TEMPLATE", Biochemistry, 32(31), 1993, pp. 7966-7971

Abstract

Intrinsic protein fluorescence of reverse transcriptases from HIV-1 and HIV-2 provides a sensitive signal for monitoring the interaction ofthe enzymes with primer/template duplex molecules. K(d) values for 18/36-mer DNA/DNA duplexes were found to be in the range of a few nanomolar (about 3 times higher for the enzyme from HIV-2 than for that fromHIV-1). The quenching of protein fluorescence induced on binding primer/template, together with an increase in extrinsic fluorescence on interaction with primer/template containing a fluorescent nucleotide at the 3'-end of the primer, was used to investigate the kinetics of interaction with reverse transcriptase from HIV-1. The results can be explained in terms of a two-step binding model, with a rapid diffusion-limited initial association (k(ass) = ca. 5 X 10(8) M-1 s-1) followed by a slow isomerization step (k = ca. 0.5 s-1). These (forward) rate constants are increased in the presence of a non-nucleoside inhibitor (S-TIBO) of HIV-1 reverse transcriptase, while the reverse rate constant for the second step is decreased, leading to an increase in affinity between the enzyme and primer/template by a factor of at least 10 when S-TIBO is bound. The results are discussed in terms of present knowledge of the structure of reverse transcriptase.

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Documento generato il 04/12/20 alle ore 22:28:29