Modomics - A Database of RNA Modifications

ID Card:

Full name: Cytoplasmic tRNA 2-thiolation protein 2
Synonym: CTU2, TUC2
GI: 125863506
Orf: N1913
COG: COG0037
UniProt: P53923
Alpha Fold Predicted Structure: AF-P53923-F1
Complex: Nsc2/Ncs6
Enzyme type: thiolase
Position of modification - modification: t:34 - mcm5s2U



Protein sequence:

MECQRCPASARNPATVESRKEKFCDECFIKFVSTKQRKQMMKDEYFRNLFKVIYPFEKEGSVSKILLPLSHSDSGSLVMLDIVHDLLLEQTKQHNNRTGFTVDVLTVFTEENVSVIKERMESLINEKMSQLNKISNIFNVHFIDVNEFFNNASEVSTFIIDNENFEIFSKSKSVDDSNILTLKEILGKYCLNNSSRSDLISIIKTQLIKHFAYENGYNAIMWGHSMTKLSEVIISLVVKGKGSQIATFLDSESFDTLNNKPCKYKNLYPMKDLLSVEIESFLQIRNLAQFLINVEETNVKPNCLIARKSLPSLGQQKLVKNMTINEITNKYFQDIQNDYSNIISTVLRTADKLTQPKSSMAKPSQCQICQSKIYTNPSNWLNRITVTSPYPVETTEEKYLFKQWQDSKLGQSHTHYVELLNEIKQGASNSLDVEDGDVKLCYGCLILLNTSIKDKNLVWPKVDTMDITANATNKNKELSQILDQFEINSDGEE

Comments:

Both Ncs2 and Ncs6 are necessary for the thiolation of U54 in cytoplasmic tRNA. The sulphur group originates from cysteine and flows through an intricate enzymatic cascade of reactions to end up as thiocarboxylated Urm1p (Urm1p-COSH) which is the substrate of 2-thiouridine formation catalysed by the complex Ncs2-Ncs6. While starting with the same cysteine desulfurase Nsf1, the rest of the sulphur relay system is different than in mitochondria. It is definitively distinct from the IscS/Tus-proteins dependent system working in bacteria. In nematode and fission yeast, Cut1-Cut2 complex are the homologs of Ncs6-Ncs2 (Tuc1-Tuc2). At variance with bacterial thiolation system, s2U formation at the wobble position 34 in tRNA can occur only after prior C5-modification of uridine ring. Ncs2 and Ncs6 are down-regulated in a proteasomal dependent fashion in yeast exposed to mild heat stress. This down-regulation influences translation of mRNAs rich in codons decoded by tRNAs thiolated by the Ncs2-Ncs6 complex.




Reaction Substrate SubstrateType Position (Anti)Codon Modified (Anti)Codon Amino Acid Change Transcript Name Transcript Region Cellular Localization References
mcm5U:mcm5s2U RNA tRNA 34 1UC 3UC tRNAGlu1UC Prokaryotic Cytosol 19151091   
mcm5U:mcm5s2U RNA tRNA 34 1UU 3UU tRNALys3UU Prokaryotic Cytosol 19151091   
mcm5U:mcm5s2U RNA tRNA 34 1UG 3UG tRNAGln1UG Prokaryotic Cytosol 19151091   
ncm5U:ncm5s2U RNA tRNA 34 &UC lUC tRNAGlu&UC Prokaryotic Cytosol
ncm5U:ncm5s2U RNA tRNA 34 &UU lUU tRNALys&UU Prokaryotic Cytosol
ncm5U:ncm5s2U RNA tRNA 34 &UG lUG tRNAGlnIUG Prokaryotic Cytosol

Alpha Fold Predicted Structure:






Clear Selection and Reset Camera

Protein sequence:

M E C Q R C P A S A R N P A T V E S R K E K F C D E C F I K F V S T K Q R K Q M M K D E Y F R N L F K V I Y P F E K E G S V S K I L L P L S H S D S G S L V M L D I V H D L L L E Q T K Q H N N R T G F T V D V L T V F T E E N V S V I K E R M E S L I N E K M S Q L N K I S N I F N V H F I D V N E F F N N A S E V S T F I I D N E N F E I F S K S K S V D D S N I L T L K E I L G K Y C L N N S S R S D L I S I I K T Q L I K H F A Y E N G Y N A I M W G H S M T K L S E V I I S L V V K G K G S Q I A T F L D S E S F D T L N N K P C K Y K N L Y P M K D L L S V E I E S F L Q I R N L A Q F L I N V E E T N V K P N C L I A R K S L P S L G Q Q K L V K N M T I N E I T N K Y F Q D I Q N D Y S N I I S T V L R T A D K L T Q P K S S M A K P S Q C Q I C Q S K I Y T N P S N W L N R I T V T S P Y P V E T T E E K Y L F K Q W Q D S K L G Q S H T H Y V E L L N E I K Q G A S N S L D V E D G D V K L C Y G C L I L L N T S I K D K N L V W P K V D T M D I T A N A T N K N K E L S Q I L D Q F E I N S D G E E

Secondary Structure Alphabet

  • G: 3-turn helix (310helix)
  • H: α-helix
  • I: 𝝅-helix (5 - turn helix)
  • T: Hydrogen Bonded Turn
  • B: β-sheet
  • S: Bend
  • C: Coil (residues not present in any of the above conformations)
  • N: Not assigned

Download PDB Structures & DSSP Secondary Structures:

Alpha Fold Pdb Files   AF-P53923-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-P53923-F1.cif  
DSSP Secondary Structures   P53923.dssp  





Publications:

Title Authors Journal Details PubMed Id DOI
Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of eukaryotic transfer RNA. Leidel S, Pedrioli PG, Bucher T, Brost R, Costanzo M, Schmidt A, Aebersold R, Boone C, Hofmann K, Peter M Nature [details] 19145231 -
Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions. Noma A, Sakaguchi Y, Suzuki T Nucleic Acids Res [details] 19151091 -
A genome-wide screen identifies genes required for formation of the wobble nucleoside 5-methoxycarbonylmethyl-2-thiouridine in Saccharomyces cerevisiae. Huang B, Lu J, Bystrom AS RNA [details] 18755837 -
Thio-modification of yeast cytosolic tRNA requires a ubiquitin-related system that resembles bacterial sulfur transfer systems. Nakai Y, Nakai M, Hayashi H J Biol Chem [details] 18664566 -
Protein degradation and dynamic tRNA thiolation fine-tune translation at elevated temperatures. Tyagi K, Pedrioli PG... Nucleic Acids Res [details] 25870413 -

Links:

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