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Mutagenesis of Gln294 of the reverse transcriptase of human immunodeficiency virus type‐2 and its effects on the ribonuclease H activity
Author(s) -
Bochner R.,
Duvshani A.,
Adir N.,
Hizi A.
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.07.010
Subject(s) - rnase h , reverse transcriptase , dna polymerase , mutagenesis , microbiology and biotechnology , ribonuclease , mutant , polymerase , rnase p , biology , virology , protein subunit , virus , dna , enzyme , wild type , polymerase chain reaction , biochemistry , rna , gene
Despite the high homology between human immunodeficiency virus type‐1 (HIV‐1) and human immunodeficiency virus type‐2 (HIV‐2) reverse transcriptases (RTs), the ribonuclease H (RNase H) level of HIV‐2 RT is lower than that of HIV‐1 RT, while the DNA polymerase of both RTs is similar. We conducted mutagenesis of HIV‐2 RT Gln294 (shown to control the RNase H activity level when modified to a Pro in the smaller p54 subunit and not in the larger p68 subunit) to various residues, and assayed the activities of all mutants. All exhibited an RNase H that is higher than the wild‐type (WT) HIV‐2 RT level, although the DNA polymerase of all mutants equals WT HIV‐2 RT level. These results represent a unique case, where every mutation induces an increase rather than a decrease in an enzyme's activity.