Recombinant DHX33 Protein Possesses Dual DNA/RNA Helicase Activity.

Abstract:

:RNA helicase DHX33 has been shown to participate in a variety of cellular activities, including ribosome biogenesis, protein translation, and gene transcription. We and others further discovered that DHX33 is strongly expressed in several types of human cancers and plays important roles in promoting cancer cell proliferation. To better understand the molecular mechanism for DHX33 in exerting its biological functions, we purified recombinant DHX33 and performed biochemical studies in vitro. DHX33 protein was found to have ATPase activity that is dependent on DNA or RNA duplexes. The ATPase activity of DHX33 is coupled with its RNA/DNA unwinding activity. If a key residue in the ATP binding site were mutated, the mutant DHX33 could not unwind DNA/RNA duplexes. Furthermore, a deletion mutant of a RKK motif previously identified to be involved in ribosome DNA binding could still unwind DNA duplexes, albeit with reduced efficiency. In summary, our study reveals that purified DHX33 protein possesses unwinding activity toward DNA and RNA duplexes.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Wang X,Ge W,Zhang Y

doi

10.1021/acs.biochem.8b00166

subject

Has Abstract

pub_date

2019-01-29 00:00:00

pages

250-258

issue

4

eissn

0006-2960

issn

1520-4995

journal_volume

58

pub_type

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