Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous Abstract"Determination of 5-hydroxymethylfurfural in honey, using headspace-solid-phase microextraction coupled with a polyoxometalate-coated piezoelectric quartz crystal"    Next Abstract"Influence of Silicon on Biocontrol Strategies to Manage Biotic Stress for Crop Protection, Performance, and Improvement" »

EMBO J


Title:"Identification of partners of TIF34, a component of the yeast eIF3 complex, required for cell proliferation and translation initiation"
Author(s):Verlhac MH; Chen RH; Hanachi P; Hershey JW; Derynck R;
Address:"Department of Growth and Development, University of California at San Francisco, San Francisco, CA 94143-0640, USA"
Journal Title:EMBO J
Year:1997
Volume:16
Issue:22
Page Number:6812 - 6822
DOI: 10.1093/emboj/16.22.6812
ISSN/ISBN:0261-4189 (Print) 1460-2075 (Electronic) 0261-4189 (Linking)
Abstract:"Eukaryotic initiation factor-3 (eIF3) in the yeast Saccharomyces cerevisiae plays a central role in initiation of translation. The eIF3 complex contains at least eight different proteins, but, as yet, little is known about the function of the individual proteins. In this study we have characterized the role of TIF34 (eIF3-p39), a recently identified WD-40 domain-containing protein of 39 kDa, in the eIF3 complex. Using temperature-sensitive mutants of TIF34 we show that this protein is required for cell cycle progression and for mating and plays an essential role in initiation of protein synthesis. By two-hybrid screening we have identified two partners that directly associate with TIF34: PRT1, a previously characterized eIF3 subunit, and a novel protein of 33 kDa (eIF3-p33) which is part of the eIF3 complex and has an RNA binding domain. TIF34 and p33 interact with each other and overexpression of p33 complements the growth defect of a tif34-ts mutant. Our results provide support for both physical and functional interactions between three subunits, TIF34, PRT1 and p33, in the eIF3 complex"
Keywords:Amino Acid Sequence Bacterial Proteins/*metabolism Base Sequence Cell Cycle Eukaryotic Initiation Factor-3 Fungal Proteins/metabolism Mating Factor Molecular Sequence Data Mutation Peptide Initiation Factors/*metabolism Peptides Protein Binding *Protein B;
Notes:"MedlineVerlhac, M H Chen, R H Hanachi, P Hershey, J W Derynck, R eng CA63101/CA/NCI NIH HHS/ GM22135/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. England 1998/01/10 EMBO J. 1997 Nov 17; 16(22):6812-22. doi: 10.1093/emboj/16.22.6812"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 22-11-2024