Revisiting tRNA chaperones: New players in an ancient game
tRNAs undergo an extensive maturation process including posttranscriptional modifications
that influence secondary and tertiary interactions. Precursor and mature tRNAs lacking key …
that influence secondary and tertiary interactions. Precursor and mature tRNAs lacking key …
[HTML][HTML] 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 …
[HTML][HTML] Crosstalk between the tRNA methyltransferase Trm1 and RNA chaperone La influences eukaryotic tRNA maturation
J Porat, A Vakiloroayaei, BM Remnant, M Talebi… - Journal of Biological …, 2023 - ASBMB
tRNAs undergo an extensive maturation process involving posttranscriptional modifications
often associated with tRNA structural stability and promoting the native fold. Impaired …
often associated with tRNA structural stability and promoting the native fold. Impaired …
[HTML][HTML] The methyl phosphate capping enzyme Bmc1/Bin3 is a stable component of the fission yeast telomerase holoenzyme
The telomerase holoenzyme is critical for maintaining eukaryotic genome integrity. In
addition to a reverse transcriptase and an RNA template, telomerase contains additional …
addition to a reverse transcriptase and an RNA template, telomerase contains additional …
[HTML][HTML] Altered tRNA processing is linked to a distinct and unusual La protein in Tetrahymena thermophila
K Kerkhofs, J Garg, É Fafard-Couture… - Nature …, 2022 - nature.com
Nascent pre-tRNAs are transcribed by RNA polymerase III and immediately bound by La
proteins on the UUU-3'OH sequence, using a tandem arrangement of the La motif and an …
proteins on the UUU-3'OH sequence, using a tandem arrangement of the La motif and an …
The fission yeast methyl phosphate capping enzyme Bmc1 guides 2′-O-methylation of the U6 snRNA
J Porat, VA Slat, SD Rader… - Nucleic Acids Research, 2023 - academic.oup.com
Splicing requires the tight coordination of dynamic spliceosomal RNAs and proteins. U6 is
the only spliceosomal RNA transcribed by RNA Polymerase III and undergoes an extensive …
the only spliceosomal RNA transcribed by RNA Polymerase III and undergoes an extensive …
The archaeal KEOPS complex possesses a functional Gon7 homolog and has an essential function independent of the cellular t6A modification level
P Wu, Q Gan, X Zhang, Y Yang, Y Xiao, Q She, J Ni… - Mlife, 2023 - Wiley Online Library
Abstract Kinase, putative Endopeptidase, and Other Proteins of Small size (KEOPS) is a
multisubunit protein complex conserved in eukaryotes and archaea. It is composed of Pcc1 …
multisubunit protein complex conserved in eukaryotes and archaea. It is composed of Pcc1 …
The fission yeast methylphosphate capping enzyme Bmc1/Bin3 promotes 2'-O-methylation of U6 and pre-mRNA splicing
J Porat, VA Slat, SD Rader, MA Bayfield - bioRxiv, 2023 - biorxiv.org
Efficient splicing requires the tight coordination of dynamic spliceosomal RNAs and proteins.
U6 is the only spliceosomal RNA transcribed by RNA Polymerase III and undergoes an …
U6 is the only spliceosomal RNA transcribed by RNA Polymerase III and undergoes an …
The methyl phosphate capping enzyme Bin3 is a stable component of the fission yeast telomerase holoenzyme
The telomerase holoenzyme is critical for maintaining eukaryotic genome integrity. In
addition to a reverse transcriptase and an RNA template, telomerase contains additional …
addition to a reverse transcriptase and an RNA template, telomerase contains additional …
[PDF][PDF] An evolutionally conserved archaeal KEOPS complex functions in DNA repair
P Wu, Q Gan, X Zhang, Y Yang, Y Xiao, Q She, J Ni… - scholar.archive.org
Double-stranded DNA break (DSB) repair is a fundamental process for all cellular life.
Recently, KEOPS, a multiple-subunit protein complex that is conserved in eukaryotes and …
Recently, KEOPS, a multiple-subunit protein complex that is conserved in eukaryotes and …