Literature DB >> 20592074

RNA 5'-triphosphatase activity of the hepatitis E virus helicase domain.

Yogesh A Karpe1, Kavita S Lole.   

Abstract

Hepatitis E virus (HEV) has a positive-sense RNA genome with a 5'-m7G cap. HEV open reading frame 1 (ORF1) encodes a polyprotein with multiple enzyme domains required for replication. HEV helicase is a nucleoside triphosphatase (NTPase) with the ability to unwind RNA duplexes in the 5'-to-3' direction. When incubated with 5'-[gamma-(32)P]RNA and 5'-[alpha-(32)P]RNA, HEV helicase released (32)P only from 5'-[gamma-(32)P]RNA, showing specificity for the gamma-beta-triphosphate bond. Removal of gamma-phosphate from the 5' end of the primary transcripts (pppRNA to ppRNA) by RNA triphosphatase is an essential step during cap formation. It is suggested that HEV employs the helicase to mediate the first step of 5' cap synthesis.

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Year:  2010        PMID： 20592074      PMCID： PMC2937651          DOI： 10.1128/JVI.00492-10

Source DB:  PubMed          Journal:  J Virol        ISSN： 0022-538X            Impact factor:   5.103


  28 in total

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Authors:  Yogesh A Karpe; Kavita S Lole
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Review 3.  Hepatitis E Virus Genome Structure and Replication Strategy.

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4.  Activities of Thrombin and Factor Xa Are Essential for Replication of Hepatitis E Virus and Are Possibly Implicated in ORF1 Polyprotein Processing.

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8.  Viral Macro Domains Reverse Protein ADP-Ribosylation.

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