TOP

Research Article

Split Viewer

Mol. Cells 2011; 31(2): 191-197

Published online December 22, 2011

https://doi.org/10.1007/s10059-011-0021-y

© The Korean Society for Molecular and Cellular Biology

Regulation of Sperm-Specific Proteins by IFE-1, a Germline-Specific Homolog of eIF4E, in C. elegans

Ichiro Kawasaki*, Myung-Hwan Jeong, and Yhong-Hee Shim*

Department of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul 143-701, Korea

Correspondence to : *Correspondence: ikawasak@mac.com (IK); yshim@konkuk.ac.kr (YHS)

Received: October 25, 2010; Revised: November 1, 2010; Accepted: November 1, 2010

Abstract

IFE-1 is one of the five C. elegans homologs of eIF4E, which is the mRNA 5' cap-binding component of the translation initiation complex eIF4F. Depletion of IFE-1 causes defects in sperm, suggesting that IFE-1 regulates a subset of genes required for sperm functions. To further understand the molecular function of IFE-1, proteomic analysis was performed to search for sperm proteins that are down-regulated in ife-1(ok1978); fem-3(q20) mutants relative to the fem-3(q20) control. The fem-3(q20) mutant background was used because it only produces sperm at restrictive temperature. Total worm proteins were subjected to 2D-DIGE, and differentially expressed protein spots were further identified by MALDI-TOF mass spectrometry. Among the identified proteins, GSP-3 and Major Sperm Proteins (MSPs) were found to be significantly down-regulated in the ife-1(ok1978) mutant. Moreover, RNAi of gsp-3 caused an ife-1-like phenotype. These results suggest that IFE-1 is required for efficient expression of some sperm-specific proteins, and the fertilization defect of ife-1 mutant is caused mainly by a reduced level of GSP-3.

Keywords Caenorhabditis elegans, eIF4E, IFE-1, proteomic analysis, sperm

Article

Research Article

Mol. Cells 2011; 31(2): 191-197

Published online February 28, 2011 https://doi.org/10.1007/s10059-011-0021-y

Copyright © The Korean Society for Molecular and Cellular Biology.

Regulation of Sperm-Specific Proteins by IFE-1, a Germline-Specific Homolog of eIF4E, in C. elegans

Ichiro Kawasaki*, Myung-Hwan Jeong, and Yhong-Hee Shim*

Department of Bioscience and Biotechnology, Bio/Molecular Informatics Center, Konkuk University, Seoul 143-701, Korea

Correspondence to:*Correspondence: ikawasak@mac.com (IK); yshim@konkuk.ac.kr (YHS)

Received: October 25, 2010; Revised: November 1, 2010; Accepted: November 1, 2010

Abstract

IFE-1 is one of the five C. elegans homologs of eIF4E, which is the mRNA 5' cap-binding component of the translation initiation complex eIF4F. Depletion of IFE-1 causes defects in sperm, suggesting that IFE-1 regulates a subset of genes required for sperm functions. To further understand the molecular function of IFE-1, proteomic analysis was performed to search for sperm proteins that are down-regulated in ife-1(ok1978); fem-3(q20) mutants relative to the fem-3(q20) control. The fem-3(q20) mutant background was used because it only produces sperm at restrictive temperature. Total worm proteins were subjected to 2D-DIGE, and differentially expressed protein spots were further identified by MALDI-TOF mass spectrometry. Among the identified proteins, GSP-3 and Major Sperm Proteins (MSPs) were found to be significantly down-regulated in the ife-1(ok1978) mutant. Moreover, RNAi of gsp-3 caused an ife-1-like phenotype. These results suggest that IFE-1 is required for efficient expression of some sperm-specific proteins, and the fertilization defect of ife-1 mutant is caused mainly by a reduced level of GSP-3.

Keywords: Caenorhabditis elegans, eIF4E, IFE-1, proteomic analysis, sperm

Mol. Cells
May 31, 2023 Vol.46 No.5, pp. 259~328
COVER PICTURE
The alpha-helices in the lamin filaments are depicted as coils, with different subdomains distinguished by various colors. Coil 1a is represented by magenta, coil 1b by yellow, L2 by green, coil 2a by white, coil 2b by brown, stutter by cyan, coil 2c by dark blue, and the lamin Ig-like domain by grey. In the background, cells are displayed, with the cytosol depicted in green and the nucleus in blue (Ahn et al., pp. 309-318).

Share this article on

  • line
  • mail

Related articles in Mol. Cells

Molecules and Cells

eISSN 0219-1032
qr-code Download