When Argonaute takes out the ribonuclease sword.
J Biol Chem
; 300(1): 105499, 2024 Jan.
Article
em En
| MEDLINE
| ID: mdl-38029964
ABSTRACT
Argonaute (AGO) proteins in all three domains of life form ribonucleoprotein or deoxyribonucleoprotein complexes by loading a guide RNA or DNA, respectively. Since all AGOs retain a PIWI domain that takes an RNase H fold, the ancestor was likely an endoribonuclease (i.e., a slicer). In animals, most miRNA-mediated gene silencing occurs slicer independently. However, the slicer activity of AGO is indispensable in specific events, such as development and differentiation, which are critical for vertebrates and thus cannot be replaced by the slicer-independent regulation. This review highlights the distinctions in catalytic activation mechanisms among slicing-competent AGOs, shedding light on the roles of two metal ions in target recognition and cleavage. The precision of the target specificity by the RNA-induced silencing complexes is reevaluated and redefined. The possible coevolutionary relationship between slicer-independent gene regulation and AGO-binding protein, GW182, is also explored. These discussions reveal that numerous captivating questions remain unanswered regarding the timing and manner in which AGOs employ their slicing activity.
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Base de dados:
MEDLINE
Assunto principal:
Ribonucleases
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Complexo de Inativação Induzido por RNA
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Proteínas Argonautas
Limite:
Animals
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article