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Title
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Proteolytic release and crystallization of the RNase H domain of human immunodeficiency virus type 1 reverse transcriptase.
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Authors
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Z.Hostomska,
D.A.Matthews,
J.F.Davies,
B.R.Nodes,
Z.Hostomsky.
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Ref.
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J Biol Chem, 1991,
266,
14697-14702.
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PubMed id
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Abstract
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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.
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