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This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.
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Yeast eIF1

IntroductionIntroduction

Translation is an essential process for both prokaryotes and eukaryotes to make various proteins from nucleic acid. It requires three different steps: initiation, elongation, and termination. Many proteins are needed in the initiation phase to form an initiation complex with the ribosome and promote the translation. In eukaryotes, these proteins are also known as eukaryotic initiation factors (eIF). The eIFs were first studied through the genetic analyzed of yeast Saccharomyces cerevisiae [1]. The initiation process is complex since it involves at least 12 eIFs containing more than 30 polypeptides , including eIF1, eIF2, eIF3, eIF4, and eIF5 [1].

PDB ID 2ogh

Drag the structure with the mouse to rotate
2ogh, 20 NMR models ()
Gene: SUI1, RFR1 (Saccharomyces cerevisiae)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structure and FunctionStructure and Function

 
Mechanism of Eukaryotic initiation

StructureStructure

eIF1 is a small protein (12 kDa) that is encode by sui1 which is one of the component of multifactor complex (MFC) that plays an important role in regulating translation initiation [2][3]. eIF1 is a universal translation factor across organisms which make eIF1 homologs can be found in other eukayotes, archaea, and some bacteria [4]. Yeast eIF1 contains a on one side with N-terminal tail (aa 1-23) or NTT [3]. It is homolog to since the structure is similar to human eIF1 (87%) with 63% matched DNA composition (identity) [4] [3]. However, yeast eIF1 has two different conformations with two clear sets of backbone resonances for 13 of the 20 residues that lead to 20 different possible solution structure of yeast eIF1 [3].


FunctionFunction

  • regulator of start site selection
  • possible figure: show where eIF1 located in the ribosome

Start Codon SelectionStart Codon Selection

stimulates the recruitment of TC to the 40s subunit

Multifactor Complex AssemblyMultifactor Complex Assembly

MechanismMechanism

overall?

eIF1-ribosome binding siteeIF1-ribosome binding site

how its bind

eIF1-eIF5 binding siteseIF1-eIF5 binding sites

  • possible green link: show binding region of eIF1 to the eIF5 --> surface representation

  • possible figure: assembly with eIF5

how it's released after AUG recognition?how it's released after AUG recognition?

  • possible figure: the release of eIF1

MutationsMutations

at the eIF1-eIF5 binding siteat the eIF1-eIF5 binding site

  • altering the basic part of eIF1-KH
  • altering the hydrophobic residues of eIF1

others?others?

ReferencesReferences

[3] [5] [4] [2] [1]

  1. ↑ 1.0 1.1 1.2 Maduzia LL, Moreau A, Poullet N, Chaffre S, Zhang Y. The role of eIF1 in translation initiation codon selection in Caenorhabditis elegans. Genetics. 2010 Dec;186(4):1187-96. Epub 2010 Sep 20. PMID:20855569 doi:10.1534/genetics.110.121541
  2. ↑ 2.0 2.1 Asano K, Sachs MS. Translation factor control of ribosome conformation during start codon selection. Genes Dev. 2007 Jun 1;21(11):1280-7. PMID:17545463 doi:10.1101/gad.1562707
  3. ↑ 3.0 3.1 3.2 3.3 3.4 Reibarkh M, Yamamoto Y, Singh CR, del Rio F, Fahmy A, Lee B, Luna RE, Ii M, Wagner G, Asano K. Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection. J Biol Chem. 2008 Jan 11;283(2):1094-103. Epub 2007 Nov 1. PMID:17974565 doi:10.1074/jbc.M708155200
  4. ↑ 4.0 4.1 4.2 Fletcher CM, Pestova TV, Hellen CU, Wagner G. Structure and interactions of the translation initiation factor eIF1. EMBO J. 1999 May 4;18(9):2631-7. PMID:10228174 doi:10.1093/emboj/18.9.2631
  5. ↑ Passmore LA, Schmeing TM, Maag D, Applefield DJ, Acker MG, Algire MA, Lorsch JR, Ramakrishnan V. The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome. Mol Cell. 2007 Apr 13;26(1):41-50. PMID:17434125 doi:10.1016/j.molcel.2007.03.018

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Edith Nurima Laban
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