URM1

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Urm1 (Ubiquitin related modifier)

Ubiquitin related modifier-1 (2qjl). In the center of protein β-grasp fold is located. Additionally, carboxy terminal glycine within a di-glycine motif is marked blue, and Mg ions are represented by black spheres.
Identifiers
Symbol URM1
Pfam PF09138
InterPro IPR015221
SCOP d.15.3.3
SUPERFAMILY d.15.3.3

Ubiquitin-related modifier-1 (URM1) is a ubiquitin related protein that modifies proteins in the yeast ubiquitin-like urmylation pathway. Structural comparisons and phylogenetic analysis of the ubiquitin superfamily has indicated that Urm1 has the most conserved structural and sequence features of the common ancestor of the entire superfamily.[1][2]

Urm1 is characterized by a core β-grasp fold and an essential carboxy terminal glycine within a di-glycine motif. Urm1 is known to be conjugated to the peroxiredoxin Ahp1, ATPBD3, and CTU2 and human MOCS3, through a mechanism involving the E1-like protein Uba4 via lysine residues.[3] Similar to ubiquitination, urmylation requires a thioester intermediate and forms isopeptide bonds between Urm1 and its substrates. Moreover, the urmylation process can be significantly enhanced by oxidative stress.[4] Functions as a protein tag with roles in nutrient sensing and oxidative stress response.

Recently it has been demonstrated that Urm1 can acts as a sulfur carrier in the thiolation of eukaryotic tRNA via a mechanism that requires the formation of a thiocarboxylated Urm1.[5] URM1 is involved in thiolation of cytoplasmic tRNAs; receives sulfur from the E1-like enzyme Uba4 and transfers it to tRNA. Sequence and structural homology studies suggest that Urm1 can be more closely linked to the prokaryotic sulphur transfer proteins, ThiS and MoaD, that can be considered as prokaryotic counterparts of the eukaryotic UBls.[6]

See also

References

  1. ↑ Xu, J.; Zhang, J.; Wang, L.; Zhou, J.; Huang, H.; Wu, J.; Zhong, Y.; Shi, Y. (2006). "Solution structure of Urm1 and its implications for the origin of protein modifiers". Proceedings of the National Academy of Sciences 103 (31): 11625–11630. doi:10.1073/pnas.0604876103. PMC 1518799. PMID 16864801. 
  2. ↑ Goehring, A. S.; Rivers, D. M.; Sprague Jr, G. F. (2003). "Urmylation: A Ubiquitin-like Pathway that Functions during Invasive Growth and Budding in Yeast". Molecular Biology of the Cell 14 (11): 4329–4341. doi:10.1091/mbc.E03-02-0079. PMC 266754. PMID 14551258. 
  3. ↑ Van Der Veen, A. G.; Schorpp, K.; Schlieker, C.; Buti, L.; Damon, J. R.; Spooner, E.; Ploegh, H. L.; Jentsch, S. (2011). "Feature Article: Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier". Proceedings of the National Academy of Sciences 108 (5): 1763–1770. doi:10.1073/pnas.1014402108. PMC 3033243. PMID 21209336. 
  4. ↑ Wang, F.; Liu, M.; Qiu, R.; Ji, C. (2011). "The dual role of ubiquitin-like protein Urm1 as a protein modifier and sulfur carrier". Protein & Cell 2 (8): 612–619. doi:10.1007/s13238-011-1074-6. PMID 21904977. 
  5. ↑ Petroski, M. D.; Salvesen, G. S.; Wolf, D. A. (2011). "Urm1 couples sulfur transfer to ubiquitin-like protein function in oxidative stress". Proceedings of the National Academy of Sciences 108 (5): 1749–1750. doi:10.1073/pnas.1019043108. PMC 3033263. PMID 21245332. 
  6. ↑ Pedrioli, Patrick; Sebastian Leidel. "Urm1 at the crossroad of modifications". EMBO reports. 
General
N terminus
C terminus
Single specific AAs
Aspartate
Glutamate
  • Transglutamination
  • C-mannosylation
Crosslinks between two AAs
  • Sulfilimine bond
Lysine-Tyrosylquinone
  • Lysine tyrosylquinone (LTQ) formation
Tryptophan-Tryptophylquinone
Three consecutive AAs
(chromophore formation)
  • p-Hydroxybenzylidene-imidazolinone formation
Crosslinks between four AAs
Chaperones/
protein folding
Heat shock proteins/
Chaperonins
Other
Protein targeting
Ubiquitin
Other
See also: posttranslational modification disorders
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)
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