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PreprintCited by 9RNA modifications and cancerRNA and protein synthesis mechanismsDNA Repair Mechanisms

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The archaeal KEOPS complex possesses a functional Gon7 homolog and has an essential function independent of cellular t 6 A modification level

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Wu, Pengju, Gan, Qi, Zhang, Xuemei, Yang, Yunfeng, Xiao, Yuanxi, She, Qunxin, Ni, Jinfeng, Huang, Qihong, Shen, Yulong·2022·mLife
DOI 10.1101/2022.08.26.505501PMC PMC10989989

Preprint — published as 10.1002/mlf2.12051 · Paper page

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Abstract

KEOPS is a multi-subunit protein complex conserved in eukaryotes and archaea. It is composed of Pcc1, Kae1, Bud32, Cgi121, and Gon7 in eukaryotes and is primarily involved in N 6 -threonylcarbamoyl adenosine (t 6 A) modification of tRNAs. Recently, KEOPS is reported to participate in homologous recombination repair in yeast. To characterize the KEOPS in archaea (aKEOPS), we conducted genetic and biochemical analyses of its encoding genes in the hyperthermophilic archaeon Saccharolobus islandicus . We show that aKEOPS also possesses five subunits, Pcc1, Kae1, Bud32, Cgi121, and Pcc1-like (or Gon7-like), just as eukaryotic KEOPS. Pcc1-like has physical interactions with Kae1 and Pcc1 and can mediate the monomerization of the dimeric subcomplex (Kae1-Pcc1-Pcc1-Kae1), suggesting that Pcc1-like is a functional homolog of the eukaryotic Gon7 subunit. Strikingly, none of the genes encoding aKEOPS subunits, including Pcc1 and Pcc1-like, can be deleted in the wild type and in a t 6 A modification complementary strain named TsaKI, implying that aKEOPS complex is essential for an additional cellular process in this archaeon. Knock-down of the Cgi121 subunit leads to severe growth retardance in the wild type which is partially rescued in TsaKI. These results suggest that aKEOPS plays an essential role independent of cellular t 6 A modification level. In addition, archaeal Cgi121 possesses dsDNA-binding activity which relies on its tRNA 3’ CCA tail binding module. Our study clarifies the subunit organization of archaeal KEOPS and suggests of an origin of eukaryotic Gon7. The study also reveals a possible link between the function in t 6 A modification and the additional function presumably homologous recombination.

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Metadata

Authors
Wu, P., Gan, Q., Zhang, X., Yang, Y., Xiao, Y., She, Q., Ni, J., Huang, Q., & Shen, Y.
Affiliations
Shandong University (CN)
Corresponding author
  • Huang, Qihong
  • Shen, Yulong
ORCID
Venue
mLife
Publisher
openRxiv
Published
2022-08-27
Volume
2
Issue
1
Pages
11-27
ISSN
2097-1699 (ISSN-L)
DOI
10.1101/2022.08.26.505501
PMC
PMC10989989
OpenAlex
W4313814059
Cited by
9
References
1
Citations by year
2026: 4 · 2025: 2 · 2024: 1 · 2023: 2
FWCI
0.80
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • mLife (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • National Natural Science Foundation of China (31771380, 2020YFA0906800, 31970546, 31670061, 31900055, 31970119)
  • National Key Research and Development Program of China (2020YFA0906800)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Keywords
KEOPS complex, tRNA modification, hyperthermophilic archaea, kAE1, homologous recombination repair, protein complex formation, essential functions

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