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Functional Characterization of an Archaeal RNase HⅡ

Author: ZhanKe
Tutor: HeZhengGuo
School: Huazhong Agricultural University
Course: Biochemistry and Molecular Biology
Keywords: Archaea Nuclease Cutting Active
CLC: Q75
Type: Master's thesis
Year: 2010
Downloads: 23
Quote: 0
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Abstract


Ribonuclease H (RNase H) is widespread in vivo of a class of nucleic acid enzymes, they are involved in the control of intracellular RNA species, quantity distribution, and RNA transcription after shearing, modification and degradation processes . Archaea is a third domain of life forms , on their function in the RNase H and mechanism is still unclear. The topics to extremely thermophilic archaea Sulfolobus tokodaii str7 the RNase H Ⅱ for the study, were analyzed in different conditions of activity , and by site-directed mutagenesis and deletion mutations identified by affecting the activity of the key amino acids , made ??possible structural mechanisms , specifically achieved the following results: ( 1 ) analysis of the archaea RNase H Ⅱ (ST0519) function of the wild-type protein identified play activity optimum reaction temperature , pH, and metal ions. ( 2 ) design point mutants, expression and purification of their mutant proteins , activity analysis found in Section 7 aspartic acid, glutamic acid No. 8 , page 195 isoleucine and leucine is 196 affect the activity of the protein amino acid positions critical . ( 3 ) design and expression and purification of the mutant protein, found in the C-terminal α helix on the ST0519 protein activity has important regulatory effects . ( 4 ) found that metal ions can stimulate the activity of the wild type protein , but it suppresses the activity of the mutant protein . This study is the first from the extremely thermophilic archaea S. tokodaii str7 identified RNase H Ⅱ ribonuclease function and catalytic mechanism . Our results confirmed the one hand, archaeal enzymes have been reported with other enzymes have similar mechanisms of action, it also found a C-terminal α helix function of the enzyme has an important influence , which is a new control mechanism . These results for the full understanding of RNase H Ⅱ protein structure, function and mechanism provides important information.

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