Ribonuclease H

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The Hepatitis B Virus Ribonuclease H Is Sensitive to Inhibitors of the Human Immunodeficiency Virus Ribonuclease H and Integrase Enzymes

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Purification and properties of ribonuclease H of calf thymus.

Ribonuclease H of calf thymus has been purified better than 3000-fold to yield an almost homogeneous preparation. The enzyme, which comprises about 0.03% of the total protein in the initial extract, is a slightly acidic protein (pI = 4.95) of molecular weight of about 64,000, possibly composed of subunits. The enzyme requires a metal ion for activation; the conditions for activation by Mg, Co, ...

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Convergent Evolution of Ribonuclease H in LTR Retrotransposons and Retroviruses

Ty3/Gypsy long terminals repeat (LTR) retrotransposons are structurally and phylogenetically close to retroviruses. Two notable structural differences between these groups of genetic elements are 1) the presence in retroviruses of an additional envelope gene, env, which mediates infection, and 2) a specific dual ribonuclease H (RNH) domain encoded by the retroviral pol gene. However, similar to...

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Thermal Adaptation of Conformational Dynamics in Ribonuclease H

The relationship between inherent internal conformational processes and enzymatic activity or thermodynamic stability of proteins has proven difficult to characterize. The study of homologous proteins with differing thermostabilities offers an especially useful approach for understanding the functional aspects of conformational dynamics. In particular, ribonuclease HI (RNase H), an 18 kD globul...

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Atomistic details of the phosphodiester cleavage of ribonuclease H

RNase H belongs to the nucleotidyl-transferase (NT) superfamily and in the presence of divalent metal ions, preferably Mg it catalyzes the hydrolysis of phosphodiester linkages of the RNA strand in the DNA:RNA hybrid duplex. RNase H activity is encoded as a part of the reverse transcriptase (RT) that converts a retroviral single strained RNA genome into double strained DNA. Due to the RNase H a...

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ژورنال

عنوان ژورنال: FEBS Journal

سال: 2009

ISSN: 1742-464X

DOI: 10.1111/j.1742-4658.2009.06906.x