Unknown

Dataset Information

0

Molecular phylogenetics and comparative modeling of HEN1, a methyltransferase involved in plant microRNA biogenesis.


ABSTRACT: BACKGROUND: Recently, HEN1 protein from Arabidopsis thaliana was discovered as an essential enzyme in plant microRNA (miRNA) biogenesis. HEN1 transfers a methyl group from S-adenosylmethionine to the 2'-OH or 3'-OH group of the last nucleotide of miRNA/miRNA* duplexes produced by the nuclease Dicer. Previously it was found that HEN1 possesses a Rossmann-fold methyltransferase (RFM) domain and a long N-terminal extension including a putative double-stranded RNA-binding motif (DSRM). However, little is known about the details of the structure and the mechanism of action of this enzyme, and about its phylogenetic origin. RESULTS: Extensive database searches were carried out to identify orthologs and close paralogs of HEN1. Based on the multiple sequence alignment a phylogenetic tree of the HEN1 family was constructed. The fold-recognition approach was used to identify related methyltransferases with experimentally solved structures and to guide the homology modeling of the HEN1 catalytic domain. Additionally, we identified a La-like predicted RNA binding domain located C-terminally to the DSRM domain and a domain with a peptide prolyl cis/trans isomerase (PPIase) fold, but without the conserved PPIase active site, located N-terminally to the catalytic domain. CONCLUSION: The bioinformatics analysis revealed that the catalytic domain of HEN1 is not closely related to any known RNA:2'-OH methyltransferases (e.g. to the RrmJ/fibrillarin superfamily), but rather to small-molecule methyltransferases. The structural model was used as a platform to identify the putative active site and substrate-binding residues of HEN and to propose its mechanism of action.

SUBMITTER: Tkaczuk KL 

PROVIDER: S-EPMC1397878 | biostudies-literature | 2006

REPOSITORIES: biostudies-literature

altmetric image

Publications

Molecular phylogenetics and comparative modeling of HEN1, a methyltransferase involved in plant microRNA biogenesis.

Tkaczuk Karolina L KL   Obarska Agnieszka A   Bujnicki Janusz M JM  

BMC evolutionary biology 20060124


<h4>Background</h4>Recently, HEN1 protein from Arabidopsis thaliana was discovered as an essential enzyme in plant microRNA (miRNA) biogenesis. HEN1 transfers a methyl group from S-adenosylmethionine to the 2'-OH or 3'-OH group of the last nucleotide of miRNA/miRNA* duplexes produced by the nuclease Dicer. Previously it was found that HEN1 possesses a Rossmann-fold methyltransferase (RFM) domain and a long N-terminal extension including a putative double-stranded RNA-binding motif (DSRM). Howeve  ...[more]

Similar Datasets

| S-EPMC10769443 | biostudies-literature
| S-EPMC6114907 | biostudies-literature
| S-EPMC1913353 | biostudies-literature
| S-EPMC4357707 | biostudies-literature
| S-EPMC2287173 | biostudies-literature
| S-EPMC5125239 | biostudies-literature
| S-EPMC5137370 | biostudies-literature
| S-EPMC3484107 | biostudies-literature
2012-01-11 | PRD000375 | Pride
| S-EPMC7143154 | biostudies-literature