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Bacterially expressed recombinant p68 RNA helicase is phosphorylated on serine, threonine, and tyrosine residues.

Abstract：

:We previously reported the expression and purification of recombinant p68 RNA helicase in a bacterial expression system. The recombinant p68 is an RNA-dependent ATPase and ATP-dependent RNA helicase. In the process of characterizing the ATPase and RNA unwinding activities of the recombinant p68, we observed that the bacterially expressed p68 RNA helicase is phosphorylated on tyrosine, serine, and threonine residues. Our data demonstrated that phosphorylations on the recombinant p68 RNA helicase affect the enzymatic activities of the protein. This is the first observation that recombinant protein expressed in bacteria Escherichia coli is phosphorylated at multiple residues by bacterial endogenous protein kinases. Our observations suggest an important mechanism in controlling the function of p68 RNA helicase by signal transduction pathways.

journal_name

Protein Expr Purif

journal_title

Protein expression and purification

authors

Yang L,Liu ZR

doi

10.1016/j.pep.2004.02.004

keywords:

subject

Has Abstract

pub_date

2004-06-01 00:00:00

pages

327-33

issue

2

eissn

1046-5928

issn

1096-0279

pii

S1046592804000786

journal_volume

35

pub_type

杂志文章

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