| 词条 | SUI1 protein domain |
| 释义 |
| Symbol = SUI1 | Name = SUI1 | image = PDB 1d1r EBI.jpg | width = | caption = NMR solution structure of E. coli yciH gene. | Pfam = PF01253 | Pfam_clan = | InterPro = IPR001950 | SMART = | PROSITE = PDOC00862 | MEROPS = | SCOP = 2if1 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} In molecular biology, the protein domain 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. FunctionSUI1 is a translation initiation factor that directs the ribosome to the translation start site, helped by eIF2 and the initiator Met-tRNAiMet.[1] 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.[2] . StructureThe 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.[3] Homologues of SUI1 have been found [4] in mammals, insects and plants. SUI1 is also evolutionary related to hypothetical proteins from Escherichia coli (yciH), Haemophilus influenzae (HI1225) and Methanococcus vannielii.[3] References1. ^{{cite journal | vauthors = Yoon HJ, Donahue TF | title = The suil suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNA(iMet) recognition of the start codon | journal = Molecular and Cellular Biology | volume = 12 | issue = 1 | pages = 248–60 | date = January 1992 | pmid = 1729602 | pmc = 364089 | doi = }} {{InterPro content|IPR001950}}2. ^{{cite journal | vauthors = Martin-Marcos P, Cheung YN, Hinnebusch AG | title = Functional elements in initiation factors 1, 1A, and 2β discriminate against poor AUG context and non-AUG start codons | journal = Molecular and Cellular Biology | volume = 31 | issue = 23 | pages = 4814–31 | date = December 2011 | pmid = 21930786 | pmc = 3232919 | doi = 10.1128/MCB.05819-11 }} 3. ^1 {{cite journal | vauthors = Herrmannová A, Daujotyte D, Yang JC, Cuchalová L, Gorrec F, Wagner S, Dányi I, Lukavsky PJ, Valásek LS | title = Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly | journal = Nucleic Acids Research | volume = 40 | issue = 5 | pages = 2294–311 | date = March 2012 | pmid = 22090426 | pmc = 3300007 | doi = 10.1093/nar/gkr765 }} 4. ^{{cite journal | vauthors = Fields C, Adams MD | title = Expressed sequence tags identify a human isolog of the suil translation initiation factor | journal = Biochemical and Biophysical Research Communications | volume = 198 | issue = 1 | pages = 288–91 | date = January 1994 | pmid = 7904817 | doi = 10.1006/bbrc.1994.1040 }} 4 : Protein domains|Protein families|Genetics|Protein biosynthesis |
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