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The hypothesized role of YbeZ in 16S rRNA maturation.
Andrews, Emma S V; Patrick, Wayne M.
Afiliação
  • Andrews ESV; Centre for Biodiscovery, School of Biological Sciences, Victoria University of Wellington, Wellington, New Zealand. emmasvandrews@gmail.com.
  • Patrick WM; Centre for Biodiscovery, School of Biological Sciences, Victoria University of Wellington, Wellington, New Zealand.
Arch Microbiol ; 204(1): 114, 2022 Jan 04.
Article em En | MEDLINE | ID: mdl-34984547
ABSTRACT
Ribosomes are the protein production machines in all living cells. Yet in contrast to our understanding of how the ribosome translates DNA information into life, the steps involved in ribosome biogenesis, the assembly of the ribosomal RNA (rRNA) and protein molecules that make up the ribosome, remain incomplete. YbeY is considered one of the most physiologically critical endoribonucleases and is implicated in numerous roles involving RNA including 16S rRNA maturation, yet our existing knowledge of its biochemical function fails to explain the phenotypes that manifest when it is lost. In bacteria, it is common for functionally associated genes to be found co-localized in the genome. Across phylogenetically diverse bacteria, the gene encoding ybeZ, encoding a PhoH domain protein, sits adjacent to ybeY. Recent experimental evidence has shown that PhoH domains are RNA helicases, suggesting that this is also the role of YbeZ. The role of an RNA helicase to support the function of YbeY would help explain its reported biochemistry; therefore, we propose a model for the function of YbeZ in 16S rRNA maturation, linking it with the most recent hypotheses on the function of YbeY, that YbeY together with other ribosomal proteins, and ribosome-associated proteins, plays a role in the biogenesis of the small ribosomal subunit. Our model provides a testable hypothesis to resolve the outstanding details surrounding ribosome biogenesis in bacteria.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Escherichia coli / Metaloproteínas Idioma: En Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Escherichia coli / Metaloproteínas Idioma: En Ano de publicação: 2022 Tipo de documento: Article