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Nucleic Acids Research, 1994, Vol. 22, No. 20 4163-4166
© 1994

MOLECULAR BIOLOGY

Eukaryotic RNAse H shares a conserved domain with caulimovirus proteins that facilitate translation of polycistronic RNA

Arcady R. Mushegian*, Herman K. Edskes and Eugene V. Koonin1

Department of Plant Pathology, University of Kentucky Lexington, KY 40546-0091, USA 1National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health Bid. 38A, 8600 Rockville Pike, Bethesda, MD 20894, US

*Io whom correspondence should be addressed at: Department of Microbiology, University of Washington, Seattle, WA 98195, USA

Received June 30, 1994. Revised September 6, 1994. Accepted September 6, 1994.

RNAse H (RNH1 protein) from the trypanosomatid Crithidia fasciculata has a functionally uncharacterized N-terminal domain dispensable for the RNAse H activity. Using computer methods for database search and multiple alignment, we show that the N-terminal domains of RNH1 and its homologue encoded by a cDNA from chicken lens are related to the conserved domain in caulimovirus ORF VI product that facilitates translation of polycistronic virus RNA in plant cells. We hypothesize that the N-terminal domain of eukaryotic RNAse H performs an as yet uncharacterized regulatory function, possibly in mRNA translation or turnover.


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