The Nature and Arrangement of Pentatricopeptide Domains and the Linker Sequences Between Them.

PPR TPR alpha helix linker repeats tricopeptide

Journal

Bioinformatics and biology insights
ISSN: 1177-9322
Titre abrégé: Bioinform Biol Insights
Pays: United States
ID NLM: 101467187

Informations de publication

Date de publication:
2020
Historique:
received: 16 01 2020
accepted: 23 01 2020
entrez: 18 3 2020
pubmed: 18 3 2020
medline: 18 3 2020
Statut: epublish

Résumé

The tricopeptide (amino acid number in the 30s) repeats constitute some of the most common amino acid repeats in proteins of diverse organisms. The most important representatives of this class are the 34-residue and 35-residue repeats, eponymously known as tetratricopeptide repeat (TPR) and pentatricopeptide repeat (PPR), respectively. The unit motif of both consists of a pair of alpha helices. As members of the large, all-helical repeat classes, TPR and PPR share structural similarities, but also play specific roles in protein function. In this study, a comprehensive bioinformatic analysis of the PPR units and the linkers that connect them was conducted. The results suggested the existence of PPR repeats of various formats, as well as smaller, PPR-unrelated repeats. Besides their length, these repeats differed in amino acid arrangements and location of key amino acids. These findings provide a broader and unified perspective of the pentatricopeptide family while raising provocative questions about the assembly and evolution of these domains.

Identifiants

pubmed: 32180683
doi: 10.1177/1177932220906434
pii: 10.1177_1177932220906434
pmc: PMC7059232
doi:

Types de publication

Journal Article

Langues

eng

Pagination

1177932220906434

Informations de copyright

© The Author(s) 2020.

Déclaration de conflit d'intérêts

Declaration of conflicting interests:The author(s) declared no potential conflicts of interest with respect to the research, authorship, and/or publication of this article.

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