J Biol Chem. 1991 Aug 5;266(22):14697-702.

Proteolytic release and crystallization of the RNase H domain of human immunodeficiency virus type 1 reverse transcriptase.

Hostomska Z, Matthews DA, Davies JF 2nd, Nodes BR, Hostomsky Z.

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Agouron Pharmaceuticals, Inc., La Jolla, California 92037.

Abstract

The RNase H domain of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase was released from recombinant DHFR-RNase H fusion protein by the action of HIV-1 protease and crystallized as large trigonal prisms that diffract x-rays to at least 2.4-A resolution. The protease cleavage occurred 18 residues away from the Phe440-Tyr441 site reported to be processed during maturation of the reverse transcriptase heterodimer. Mutagenesis of the protease-sensitive region (residues 430-440), which is part of the crystallized domain, indicates that any alteration of the wild-type sequence results in increased proteolysis of the p66 subunit. A model of asymmetric processing in HIV-1 reserve transcriptase which involves partial unfolding of the RNase H domain is proposed based on these results and the recently reported three-dimensional structure of this domain.

PMID:: 1713588; [PubMed - indexed for MEDLINE]

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Research Support, U.S. Gov't, P.H.S.

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GM-39599/GM/NIGMS NIH HHS/United States

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Cited by 5 PubMed Central articles

The mutation T477A in HIV-1 reverse transcriptase (RT) restores normal proteolytic processing of RT in virus with Gag-Pol mutated in the p51-RNH cleavage site. [Retrovirology. 2010]
The mutation T477A in HIV-1 reverse transcriptase (RT) restores normal proteolytic processing of RT in virus with Gag-Pol mutated in the p51-RNH cleavage site.
Abram ME, Sarafianos SG, Parniak MA. Retrovirology. 2010 Feb 1; 7:6. Epub 2010 Feb 1.
Virion instability of human immunodeficiency virus type 1 reverse transcriptase (RT) mutated in the protease cleavage site between RT p51 and the RT RNase H domain. [J Virol. 2005]
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Abram ME, Parniak MA. J Virol. 2005 Sep; 79(18):11952-61.
Hydroxyl radical footprint analysis of human immunodeficiency virus reverse transcriptase-template.primer complexes. [Proc Natl Acad Sci U S A. 1993]
Hydroxyl radical footprint analysis of human immunodeficiency virus reverse transcriptase-template.primer complexes.
Metzger W, Hermann T, Schatz O, Le Grice SF, Heumann H. Proc Natl Acad Sci U S A. 1993 Jul 1; 90(13):5909-13.

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Structures reported by this article

Crystal Structure Of The Ribonuclease H Domain Of Hiv-1 Reverse Transcriptase

PDB: 1HRH

Source: Human immunodeficiency virus 1

Method: X-Ray Diffraction

Resolution: 2.4 Å

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