Biology:SUI1
| SUI1 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 NMR solution structure of E. coli yciH gene. | |||||||||
| Identifiers | |||||||||
| Symbol | SUI1 | ||||||||
| Pfam | PF01253 | ||||||||
| InterPro | IPR001950 | ||||||||
| PROSITE | PDOC00862 | ||||||||
| SCOP2 | 2if1 / SCOPe / SUPFAM | ||||||||
| |||||||||
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]
Function
SUI1 is a translation initiation factor that directs the ribosome to the translation start site, helped by eIF2 and the initiator Met-tRNAiMet.[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
- ↑ Prokaryotic+Initiation+Factor-3 at the US National Library of Medicine Medical Subject Headings (MeSH)
- ↑ "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. January 1992. doi:10.1128/mcb.12.1.248. PMID 1729602.
- ↑ "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. December 2011. doi:10.1128/MCB.05819-11. PMID 21930786.
- ↑ Osterman, IA; Evfratov, SA; Dzama, MM; Pletnev, PI; Kovalchuk, SI; Butenko, IO; Pobeguts, OV; Golovina, AY et al. (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. PMID 26177339.
- ↑ 5.0 5.1 "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. March 2012. doi:10.1093/nar/gkr765. PMID 22090426.
- ↑ "Expressed sequence tags identify a human isolog of the suil translation initiation factor". Biochemical and Biophysical Research Communications 198 (1): 288–91. January 1994. doi:10.1006/bbrc.1994.1040. PMID 7904817.
 |  |
