SUI1

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SUI1
PDB 1d1r EBI.jpg
NMR solution structure of E. coli yciH gene.
Identifiers
SymbolSUI1
Pfam PF01253
InterPro IPR001950
PROSITE PDOC00862
SCOP2 2if1 / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

In molecular biology, the single-domain protein SUI1 is a translation initiation factor often found in the fungus, Saccharomyces cerevisiae (Baker's yeast) but it is also found in other eukaryotes and prokaryotes as well as archaea. It is otherwise known as Eukaryotic translation initiation factor 1 (eIF1) in eukaryotes or YciH in bacteria. [1]

Contents

Function

SUI1 is a translation initiation factor that directs the ribosome to the translation start site, helped by eIF2 and the initiator Met-tRNA iMet. [2] SUI1 ensures that translation initiation commences from the correct start codon (usually AUG), by stabilizing the pre-initiation complex around the start codon. SUI1 promotes a high initiation fidelity for the AUG codon, discriminating against non-AUG codons. [3]

In E. coli however, it seems that the SUI1 homolog YciH is an inhibitor of translation during stress instead. [4]

Structure

The primary structure of the SUI1 protein is made up of 108 amino acids. The protein domain has a structure made of a seven-bladed beta-propeller and it also contains a C-terminal alpha helix. [5] Homologues of SUI1 have been found [6] in mammals, insects and plants. SUI1 is also evolutionary related to proteins from Escherichia coli (yciH), Haemophilus influenzae (HI1225) and Methanococcus vannielii. [5]

References

  1. ↑ Prokaryotic+Initiation+Factor-3 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  2. ↑ Yoon HJ, Donahue TF (January 1992). "The suil suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNA(iMet) recognition of the start codon". Molecular and Cellular Biology. 12 (1): 248–60. doi:10.1128/mcb.12.1.248. PMC   364089 . PMID   1729602.
  3. ↑ Martin-Marcos P, Cheung YN, Hinnebusch AG (December 2011). "Functional elements in initiation factors 1, 1A, and 2β discriminate against poor AUG context and non-AUG start codons". Molecular and Cellular Biology. 31 (23): 4814–31. doi:10.1128/MCB.05819-11. PMC   3232919 . PMID   21930786.
  4. ↑ Osterman, IA; Evfratov, SA; Dzama, MM; Pletnev, PI; Kovalchuk, SI; Butenko, IO; Pobeguts, OV; Golovina, AY; Govorun, VM; Bogdanov, AA; Sergiev, PV; Dontsova, OA (2015). "A bacterial homolog YciH of eukaryotic translation initiation factor eIF1 regulates stress-related gene expression and is unlikely to be involved in translation initiation fidelity". RNA Biology. 12 (9): 966–71. doi:10.1080/15476286.2015.1069464. PMC   4615754 . PMID   26177339.
  5. 1 2 Herrmannová A, Daujotyte D, Yang JC, Cuchalová L, Gorrec F, Wagner S, Dányi I, Lukavsky PJ, Valásek LS (March 2012). "Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly". Nucleic Acids Research. 40 (5): 2294–311. doi:10.1093/nar/gkr765. PMC   3300007 . PMID   22090426.
  6. ↑ Fields C, Adams MD (January 1994). "Expressed sequence tags identify a human isolog of the suil translation initiation factor". Biochemical and Biophysical Research Communications. 198 (1): 288–91. Bibcode:1994BBRC..198..288F. doi:10.1006/bbrc.1994.1040. PMID   7904817.
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