The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis.
The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis.
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核仁蛋白ESF2与DEXD/H盒RNA解旋酶DBP8直接相互作用,以刺激ATP水解。
DOI:
10.1093/nar/gkl419
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发表时间:
2006
影响因子:
14.9
通讯作者:
Baserga SJ
中科院分区:
文献类型:
--
作者:
Granneman S;Lin C;Champion EA;Nandineni MR;Zorca C;Baserga SJ
While 18 putative RNA helicases are involved in ribosome biogenesis in Saccharomyces cerevisiae, their enzymatic properties have remained largely biochemically uncharacterized. To better understand their function, we examined the enzymatic properties of Dpb8, a DExD/H box protein previously shown to be required for the synthesis of the 18S rRNA. As expected for an RNA helicase, we demonstrate that recombinant Dbp8 has ATPase activity in vitro, and that this activity is dependent on an intact ATPase domain. Strikingly, we identify Esf2, a nucleolar putative RNA binding protein, as a binding partner for Dbp8, and show that it enhances Dbp8 ATPase activity by decreasing the KM for ATP. Thus, we have uncovered Esf2 as the first example of a protein co-factor that has a stimulatory effect on a nucleolar RNA helicase. We show that Esf2 can bind to pre-rRNAs and speculate that it may function to bring Dbp8 to the pre-rRNA, thereby both regulating its enzymatic activity and guiding Dbp8 to its site of action.
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影响因子:
5.3
作者:
Granneman, S;Bernstein, KA;Baserga, SJ
通讯作者:
Baserga, SJ
影响因子:
10.5
作者:
Oberer, M;Marintchev, A;Wagner, G
通讯作者:
Wagner, G
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14.9
作者:
Daugeron, ML;Linder, P
通讯作者:
Linder, P
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5.3
作者:
Hoang, T;Peng, WT;Lafontaine, DLJ
通讯作者:
Lafontaine, DLJ
影响因子:
56.9
作者:
Fairman, ME;Maroney, PA;Jankowsky, E
通讯作者:
Jankowsky, E