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Gene Review

rnh1  -  ribonuclease H1

Drosophila melanogaster

Synonyms: 74/9, CG8729, Dmel\CG8729, RNase H1, RnH1, ...
 
 
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Disease relevance of rnh1

 

High impact information on rnh1

  • Although they share a similar overall fold related to ribonucleases of the RNase H family, they have local differences at the putative active site [5].
  • The jockey polymerase demonstrates RNA and DNA-directed DNA polymerase activities but lacks detectable RNase H, has a temperature optimum at 26 degrees C, requires Mg2+ or Mn2+ as a cofactor and is inactivated by sulphydryl reagent [6].
  • The Drosophila polymerase-primase contains neither 3'-5' exonuclease nor RNase H-like activities, and catalyzes no significant pyrophosphate exchange [7].
  • Using the enzyme ribonuclease H, we show that this size decrease is a result of a progressively shorter poly(A) tract and suggest that these transcripts undergo an active sequential shortening of their poly(A) tracts in prepupal salivary glands [8].
  • Comparison of Drosophila RNase H1 amino acid sequence to that of other cellular eukaryotic homologs reveals the presence of three evolutionarily distinct domains [1].
 

Biological context of rnh1

  • Analysis of the developmental and spatial expression profiles of a reporter gene placed under the control of the RNase H1 promoter revealed increased expression in several larval tissues [9].
  • However, disruption of the RNase H1 gene does not affect proliferation, but probably alters the regulation of gene expression [9].
  • The lethal phenotype of this mutant also demonstrates that RNase H1 activity in Drosophila cannot be provided by other cellular RNase H activities [9].
  • In addition, Ulysses contains protease, reverse transcriptase, RNase H and integrase domains encoded in the second open reading frame [10].
 

Associations of rnh1 with chemical compounds

References

  1. Functional characterization of RNase H1 from Drosophila melanogaster. Filippov, V., Filippova, M., Gill, S.S. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  2. MosquI, a novel family of mosquito retrotransposons distantly related to the Drosophila I factors, may consist of elements of more than one origin. Tu, Z., Hill, J.J. Mol. Biol. Evol. (1999) [Pubmed]
  3. Alpha-anomeric DNA: beta-RNA hybrids as new synthetic inhibitors of Escherichia coli RNase H, Drosophila embryo RNase H and M-MLV reverse transcriptase. Bloch, E., Lavignon, M., Bertrand, J.R., Pognan, F., Morvan, F., Malvy, C., Rayner, B., Imbach, J.L., Paoletti, C. Gene (1988) [Pubmed]
  4. Molecular characterization and genomic distribution of Isis: a new retrotransposon of Drosophila buzzatii. Guerreiro, M.P., Fontdevila, A. Mol. Genet. Genomics (2007) [Pubmed]
  5. Structures of the PIN domains of SMG6 and SMG5 reveal a nuclease within the mRNA surveillance complex. Glavan, F., Behm-Ansmant, I., Izaurralde, E., Conti, E. EMBO J. (2006) [Pubmed]
  6. Authentic reverse transcriptase is coded by jockey, a mobile Drosophila element related to mammalian LINEs. Ivanov, V.A., Melnikov, A.A., Siunov, A.V., Fodor, I.I., Ilyin, Y.V. EMBO J. (1991) [Pubmed]
  7. The DNA polymerase-primase from drosophila melanogaster embryos. Rate and fidelity of polymerization on single-stranded DNA templates. Kaguni, L.S., DiFrancesco, R.A., Lehman, I.R. J. Biol. Chem. (1984) [Pubmed]
  8. Poly(A) shortening of coregulated transcripts in Drosophila. Restifo, L.L., Guild, G.M. Dev. Biol. (1986) [Pubmed]
  9. Drosophila RNase H1 is essential for development but not for proliferation. Filippov, V., Filippov, M., Gill, S.S. Mol. Genet. Genomics (2001) [Pubmed]
  10. Ulysses transposable element of Drosophila shows high structural similarities to functional domains of retroviruses. Evgen'ev, M.B., Corces, V.G., Lankenau, D.H. J. Mol. Biol. (1992) [Pubmed]
  11. Mechanism of Mos1 transposition: insights from structural analysis. Richardson, J.M., Dawson, A., O'Hagan, N., Taylor, P., Finnegan, D.J., Walkinshaw, M.D. EMBO J. (2006) [Pubmed]
 
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