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Gene Review

rnhA  -  ribonuclease H

Thermus thermophilus HB27

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Disease relevance of TTC1191

  • Stability parameters for individual residues in Thermus thermophilus cysteine-free RNase H were determined by native state hydrogen exchange, thus providing a unique comparison of regional thermodynamics between thermophilic and mesophilic homologues [1].
  • E. coli strain MIC3001, which shows an RNase H-dependent, temperature-sensitive growth phenotype, was used for this purpose [2].

High impact information on TTC1191

  • As an initial step to elucidate the stabilization mechanism of the thermophilic RNase H, we examined whether certain regions in its amino acid sequence confer the thermostability [3].
  • A Gly residue inserted between alpha-helices B and C appears to relieve unfavorable interactions in the transition state and alternate conformer(s) and represents an important adaptation to adjust conformational changes within RNase H for activity at high temperatures [4].
  • Furthermore, heat treatment of the fusion enzyme showed that it was stable as a tetramer at 65 degrees C. The fusion enzyme was shown to have both biotin binding and RNase H catalytic properties [5].
  • A streptavidin-RNase H gene fusion was constructed by cloning the Thermus thermophilus RNase H coding sequence in the streptavidin expression vector pTSA18F [5].


  1. Structural distribution of stability in a thermophilic enzyme. Hollien, J., Marqusee, S. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  2. A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. Haruki, M., Noguchi, E., Akasako, A., Oobatake, M., Itaya, M., Kanaya, S. J. Biol. Chem. (1994) [Pubmed]
  3. Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. Kimura, S., Nakamura, H., Hashimoto, T., Oobatake, M., Kanaya, S. J. Biol. Chem. (1992) [Pubmed]
  4. An inserted Gly residue fine tunes dynamics between mesophilic and thermophilic ribonucleases H. Butterwick, J.A., Palmer, A.G. Protein Sci. (2006) [Pubmed]
  5. Cycling probe technology with RNase H attached to an oligonucleotide. Bekkaoui, F., Poisson, I., Crosby, W., Cloney, L., Duck, P. BioTechniques (1996) [Pubmed]
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