Nucleic Acids Research, 2003, Vol. 31, No. 7 1830-1837
© 2003 Oxford University Press
Scp160p associates with specific mRNAs in yeast
Department of Human Genetics, Emory University School of Medicine, 615 Michael Street, Atlanta, GA 30322, USA
*To whom correspondence should be addressed. Tel: +1 404 727 3924; Fax: +1 404 727 3949; Email: jfridov{at}emory.edu
Scp160p is a multiple KH-domain RNA-binding protein in yeast that has been demonstrated previously to associate with both soluble and membrane-bound polyribosomes as an mRNP component. One key question that has remained unanswered, however, is whether the mRNAs in these mRNP complexes are random or specific. We have addressed this question using microarray analyses of RNAs released from affinity isolated Scp160p-containing complexes, compared with total RNA controls from the same lysates. Our results, confirmed by quantitative RTPCR analysis, clearly demonstrate that Scp160p associates with specific rather than with random messages, and that among the enriched targets are DHH1, YOR338W, BIK1, YOL155C and NAM8. Furthermore, loss of Scp160p resulted in a significant change in both the abundance and distribution between soluble and membrane-associated fractions for at least one of these messages (YOR338W), and in a subtle yet significant shift from soluble polyribosomes to soluble mRNPs for at least two of these target messages (DHH1 and YOR338W). Together, these data not only identify specific mRNA targets associated with Scp160p in vivo, they demonstrate that the association of Scp160p with these messages is biologically relevant.
![]()
CiteULike
Connotea
Del.icio.us What's this?
This article has been cited by other articles:
![]() |
B. Sezen, M. Seedorf, and E. Schiebel The SESA network links duplication of the yeast centrosome with the protein translation machinery Genes & Dev., July 1, 2009; 23(13): 1559 - 1570. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. A. Brykailo, L. M. McLane, J. Fridovich-Keil, and A. H. Corbett Analysis of a predicted nuclear localization signal: implications for the intracellular localization and function of the Saccharomyces cerevisiae RNA-binding protein Scp160 Nucleic Acids Res., November 29, 2007; 35(20): 6862 - 6869. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. R. Nelson, H. Luo, H. K. Vari, B. J. Cox, A. J. Simmonds, H. M. Krause, H. D. Lipshitz, and C. A. Smibert A Multiprotein Complex That Mediates Translational Enhancement in Drosophila J. Biol. Chem., November 23, 2007; 282(47): 34031 - 34038. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. A. Brykailo, A. H. Corbett, and J. L. Fridovich-Keil Functional overlap between conserved and diverged KH domains in Saccharomyces cerevisiae SCP160 Nucleic Acids Res., February 28, 2007; 35(4): 1108 - 1118. [Abstract] [Full Text] [PDF] |
||||
![]() |
F.-X. Marsellach, D. Huertas, and F. Azorin The Multi-KH Domain Protein of Saccharomyces cerevisiae Scp160p Contributes to the Regulation of Telomeric Silencing J. Biol. Chem., June 30, 2006; 281(26): 18227 - 18235. [Abstract] [Full Text] [PDF] |
||||
![]() |
H. Hieronymus and P. A. Silver A systems view of mRNP biology Genes & Dev., December 1, 2004; 18(23): 2845 - 2860. [Abstract] [Full Text] [PDF] |
||||
![]() |
A.-m. Li, C. A. Vargas, M. A. Brykailo, K. K. Openo, A. H. Corbett, and J. L. Fridovich-Keil Both KH and non-KH domain sequences are required for polyribosome association of Scp160p in yeast Nucleic Acids Res., September 8, 2004; 32(16): 4768 - 4775. [Abstract] [Full Text] [PDF] |
||||
![]() |
T. J. Westmoreland, J. R. Marks, J. A. Olson Jr., E. M. Thompson, M. A. Resnick, and C. B. Bennett Cell Cycle Progression in G1 and S Phases Is CCR4 Dependent following Ionizing Radiation or Replication Stress in Saccharomyces cerevisiae Eukaryot. Cell, April 1, 2004; 3(2): 430 - 446. [Abstract] [Full Text] [PDF] |
||||
![]() |
B. A. Mendelsohn, A.-m. Li, C. A. Vargas, K. Riehman, A. Watson, and J. L. Fridovich-Keil Genetic and biochemical interactions between SCP160 and EAP1 in yeast Nucleic Acids Res., October 15, 2003; 31(20): 5838 - 5847. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. M. Goolsby and D. J. Shapiro RNAi-mediated depletion of the 15 KH domain protein, vigilin, induces death of dividing and non-dividing human cells but does not initially inhibit protein synthesis Nucleic Acids Res., October 1, 2003; 31(19): 5644 - 5653. [Abstract] [Full Text] [PDF] |
||||



