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Solution structure of the Drosha double-stranded RNA-binding domain.


ABSTRACT:

Background

Drosha is a nuclear RNase III enzyme that initiates processing of regulatory microRNA. Together with partner protein DiGeorge syndrome critical region 8 (DGCR8), it forms the Microprocessor complex, which cleaves precursor transcripts called primary microRNA to produce hairpin precursor microRNA. In addition to two RNase III catalytic domains, Drosha contains a C-terminal double-stranded RNA-binding domain (dsRBD). To gain insight into the function of this domain, we determined the nuclear magnetic resonance (NMR) solution structure.

Results

We report here the solution structure of the dsRBD from Drosha (Drosha-dsRBD). The alphabetabetabetaalpha fold is similar to other dsRBD structures. A unique extended loop distinguishes this domain from other dsRBDs of known structure.

Conclusions

Despite uncertainties about RNA-binding properties of the Drosha-dsRBD, its structure suggests it retains RNA-binding features. We propose that this domain may contribute to substrate recognition in the Drosha-DGCR8 Microprocessor complex.

SUBMITTER: Mueller GA 

PROVIDER: S-EPMC2836000 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature

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Publications

Solution structure of the Drosha double-stranded RNA-binding domain.

Mueller Geoffrey A GA   Miller Matthew T MT   DeRose Eugene F EF   Ghosh Mahua M   London Robert E RE   Hall Traci M Tanaka TMT  

Silence 20100112 1


<h4>Background</h4>Drosha is a nuclear RNase III enzyme that initiates processing of regulatory microRNA. Together with partner protein DiGeorge syndrome critical region 8 (DGCR8), it forms the Microprocessor complex, which cleaves precursor transcripts called primary microRNA to produce hairpin precursor microRNA. In addition to two RNase III catalytic domains, Drosha contains a C-terminal double-stranded RNA-binding domain (dsRBD). To gain insight into the function of this domain, we determine  ...[more]

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