HEPN RNases - an emerging class of functionally distinct RNA processing and degradation enzymes.

Pillon, Monica C; Gordon, Jacob; Frazier, Meredith N; Stanley, Robin E

Pillon, Monica C; Gordon, Jacob; Frazier, Meredith N; Stanley, Robin E.

Afiliación

Pillon MC; Department of Health and Human Services, Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC, USA.
Gordon J; Department of Health and Human Services, Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC, USA.
Frazier MN; Department of Health and Human Services, Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC, USA.
Stanley RE; Department of Health and Human Services, Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC, USA.

Crit Rev Biochem Mol Biol ; 56(1): 88-108, 2021 02.

Article en En | MEDLINE | ID: mdl-33349060

RESUMEN

HEPN (Higher Eukaryotes and Prokaryotes Nucleotide-binding) RNases are an emerging class of functionally diverse RNA processing and degradation enzymes. Members are defined by a small α-helical bundle encompassing a short consensus RNase motif. HEPN dimerization is a universal requirement for RNase activation as the conserved RNase motifs are precisely positioned at the dimer interface to form a composite catalytic center. While the core HEPN fold is conserved, the organization surrounding the HEPN dimer can support large structural deviations that contribute to their specialized functions. HEPN RNases are conserved throughout evolution and include bacterial HEPN RNases such as CRISPR-Cas and toxin-antitoxin associated nucleases, as well as eukaryotic HEPN RNases that adopt large multi-component machines. Here we summarize the canonical elements of the growing HEPN RNase family and identify molecular features that influence RNase function and regulation. We explore similarities and differences between members of the HEPN RNase family and describe the current mechanisms for HEPN RNase activation and inhibition.

Asunto(s)

Endorribonucleasas/metabolismo; Proteolisis; Procesamiento Postranscripcional del ARN; Proteínas de Unión al ARN/metabolismo; Secuencia de Aminoácidos; Animales; Sistemas CRISPR-Cas; Dominio Catalítico; Endorribonucleasas/química; Endorribonucleasas/genética; Humanos; Conformación Proteica en Hélice alfa; Multimerización de Proteína; Estabilidad del ARN; Proteínas de Unión al ARN/química; Proteínas de Unión al ARN/genética; Sistemas Toxina-Antitoxina

Palabras clave

CRISPR-Cas; Endoribonuclease; HEPN; NiKs; RNA degradation; RNA processing; Toxin-Antitoxin

Texto completo

Añadir a Mi BVS

Imprimir

XML

PubMed Links

Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Procesamiento Postranscripcional del ARN / Proteínas de Unión al ARN / Endorribonucleasas / Proteolisis Límite: Animals / Humans Idioma: En Revista: Crit Rev Biochem Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR / BIOQUIMICA Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido

Texto completo

Añadir a Mi BVS

Imprimir

XML

PubMed Links

Buscar en Google