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

Autor:	B.R. Nodes, Z. Hostomsky, Z. Hostomska, J.F. Davies nd, D.A. Matthews
Rok vydání:	1991
Předmět:	Protease medicine.medical_treatment Protein subunit Cell Biology Biology Cleavage (embryo) Biochemistry Fusion protein Molecular biology Reverse transcriptase law.invention law medicine biology.protein Recombinant DNA RNase H Molecular Biology Peptide sequence
Zdroj:	Journal of Biological Chemistry. 266:14697-14702
ISSN:	0021-9258
DOI:	10.1016/s0021-9258(18)98742-9
Popis:	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.
Databáze:	OpenAIRE
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