A substrate binding model for the KEOPS tRNA modifying complex
The KEOPS complex, which is conserved across archaea and eukaryotes, is composed of
four core subunits; Pcc1, Kae1, Bud32 and Cgi121. KEOPS is crucial for the fitness of all …
four core subunits; Pcc1, Kae1, Bud32 and Cgi121. KEOPS is crucial for the fitness of all …
A paralog of Pcc1 is the fifth core subunit of the KEOPS tRNA-modifying complex in Archaea
MC Daugeron, S Missoury, V Da Cunha… - Nature …, 2023 - nature.com
Abstract In Archaea and Eukaryotes, the synthesis of a universal tRNA modification, N6-
threonyl-carbamoyl adenosine (t6A), is catalyzed by the KEOPS complex composed of …
threonyl-carbamoyl adenosine (t6A), is catalyzed by the KEOPS complex composed of …
Proteomic analysis of the human KEOPS complex identifies C14ORF142 as a core subunit homologous to yeast Gon7
LCK Wan, P Maisonneuve, RK Szilard… - Nucleic acids …, 2017 - academic.oup.com
The KEOPS/EKC complex is a tRNA modification complex involved in the biosynthesis of N6-
threonylcarbamoyladenosine (t6A), a universally conserved tRNA modification found on …
threonylcarbamoyladenosine (t6A), a universally conserved tRNA modification found on …
Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex
The yeast KEOPS protein complex comprising Kae1, Bud32, Cgi121, Pcc1 and Gon7 is
responsible for the essential tRNA threonylcarbamoyladenosine (t6A) modification. Deletion …
responsible for the essential tRNA threonylcarbamoyladenosine (t6A) modification. Deletion …
The structural and functional workings of KEOPS
J Beenstock, F Sicheri - Nucleic Acids Research, 2021 - academic.oup.com
Abstract KEOPS (K inase, E ndopeptidase and O ther P roteins of S mall size) is a five-
subunit protein complex that is highly conserved in eukaryotes and archaea and is essential …
subunit protein complex that is highly conserved in eukaryotes and archaea and is essential …
Molecular basis of A. thaliana KEOPS complex in biosynthesizing tRNA t6A
X Zheng, C Su, L Duan, M Jin, Y Sun… - Nucleic Acids …, 2024 - academic.oup.com
In archaea and eukaryotes, the evolutionarily conserved KEOPS is composed of four core
subunits―Kae1, Bud32, Cgi121 and Pcc1, and a fifth Gon7/Pcc2 that is found in fungi and …
subunits―Kae1, Bud32, Cgi121 and Pcc1, and a fifth Gon7/Pcc2 that is found in fungi and …
Structural and functional characterization of KEOPS dimerization by Pcc1 and its role in t6A biosynthesis
LCK Wan, MC Pillon, N Thevakumaran… - Nucleic acids …, 2016 - academic.oup.com
KEOPS is an ancient protein complex required for the biosynthesis of N6-
threonylcarbamoyladenosine (t6A), a universally conserved tRNA modification found on all …
threonylcarbamoyladenosine (t6A), a universally conserved tRNA modification found on all …
Gcn4 misregulation reveals a direct role for the evolutionary conserved EKC/KEOPS in the t6A modification of tRNAs
MC Daugeron, TL Lenstra, M Frizzarin… - Nucleic acids …, 2011 - academic.oup.com
The EKC/KEOPS complex is universally conserved in Archaea and Eukarya and has been
implicated in several cellular processes, including transcription, telomere homeostasis and …
implicated in several cellular processes, including transcription, telomere homeostasis and …
The highly conserved KEOPS/EKC complex is essential for a universal tRNA modification, t6A
The highly conserved Kinase, Endopeptidase and Other Proteins of small Size (KEOPS)/
Endopeptidase‐like and Kinase associated to transcribed Chromatin (EKC) protein complex …
Endopeptidase‐like and Kinase associated to transcribed Chromatin (EKC) protein complex …
Sua5 catalyzing universal t6A tRNA modification is responsible for multifaceted functions of the KEOPS complex in Cryptococcus neoformans
Y Choi, H Hyeon, K Lee, YS Bahn - Msphere, 2024 - Am Soc Microbiol
The N6-threonylcarbamoyl adenosine (t6A) tRNA modification is critical for ensuring
translation fidelity across three domains of life. Our prior work highlighted the KEOPS …
translation fidelity across three domains of life. Our prior work highlighted the KEOPS …