Genetic Insight into the Domain Structure and Functions of Dicer-Type Ribonucleases.
DCL proteins
DUF283
Dicer
PAZ
RNA binding proteins
RNAi
RNase III
dsRBD
helicase
ribonuclease III
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
09 Jan 2021
09 Jan 2021
Historique:
received:
30
11
2020
revised:
05
01
2021
accepted:
06
01
2021
entrez:
13
1
2021
pubmed:
14
1
2021
medline:
8
9
2021
Statut:
epublish
Résumé
Ribonuclease Dicer belongs to the family of RNase III endoribonucleases, the enzymes that specifically hydrolyze phosphodiester bonds found in double-stranded regions of RNAs. Dicer enzymes are mostly known for their essential role in the biogenesis of small regulatory RNAs. A typical Dicer-type RNase consists of a helicase domain, a domain of unknown function (DUF283), a PAZ (Piwi-Argonaute-Zwille) domain, two RNase III domains, and a double-stranded RNA binding domain; however, the domain composition of Dicers varies among species. Dicer and its homologues developed only in eukaryotes; nevertheless, the two enzymatic domains of Dicer, helicase and RNase III, display high sequence similarity to their prokaryotic orthologs. Evolutionary studies indicate that a combination of the helicase and RNase III domains in a single protein is a eukaryotic signature and is supposed to be one of the critical events that triggered the consolidation of the eukaryotic RNA interference. In this review, we provide the genetic insight into the domain organization and structure of Dicer proteins found in vertebrate and invertebrate animals, plants and fungi. We also discuss, in the context of the individual domains, domain deletion variants and partner proteins, a variety of Dicers' functions not only related to small RNA biogenesis pathways.
Identifiants
pubmed: 33435485
pii: ijms22020616
doi: 10.3390/ijms22020616
pmc: PMC7827160
pii:
doi:
Substances chimiques
Ribonuclease III
EC 3.1.26.3
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Polish National Science Centre
ID : SONATA BIS 2016/22/E/NZ1/00422
Organisme : The National Centre for Research and Development
ID : POWR.03.02.00-00-I011/16
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