Nucleic Acids Research, 2000, Vol. 28, No. 7 1576-1584
© 2000 Oxford University Press
Scp160p, a multiple KH-domain protein, is a component of mRNP complexes in yeast
Graduate Program in Biochemistry, Cell and Developmental Biology, Emory University, Atlanta, GA, USA and 1Department of Genetics, Room 429C, Dental Building, Emory University School of Medicine, 1462 Clifton Road NE, Atlanta, GA 30322, USA
Scp160p is a 160 kDa protein in the yeast Saccharomyces cerevisiae that contains 14 repeats of the hnRNP K-homology (KH) domain, and demonstrates significant sequence homology to a family of proteins collectively known as vigilins. As a first step towards defining the function of Scp160p, we have characterized the subcellular distribution and in vivo interactions of this protein. Using sucrose gradient fractionation studies we have demonstrated that Scp160p in cytoplasmic lysates is predominantly associated with polyribosomes. Furthermore, we have found that Scp160p is released from polyribosomes by EDTA in the form of a large complex of 
1300 kDa that is sensitive both to RNase and NaCl. Using affinity-chromatography to isolate these complexes, we have identified two protein components other than Scp160p: poly(A) binding protein, Pab1p, and Bfr1p. The presence of Pab1p confirms these complexes to be mRNPs. The presence of Bfr1p is intriguing because the null phenotype for this gene is essentially the same as that reported for scp160-null cells: increased cell size and aberrant DNA content. These results demonstrate that Scp160p associates with polyribosome-bound mRNP complexes in vivo, implicating a role for this protein in one or more levels of mRNA metabolism in yeast.
* To whom correspondence should be addressed. Tel: +1 404 727 3924; Fax: +1 404 727 3949; Email: jfridov@emory.edu
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  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]
|
|
|
|
 |
|
 S. A. Chasse, P. Flanary, S. C. Parnell, N. Hao, J. Y. Cha, D. P. Siderovski, and H. G. Dohlman Genome-Scale Analysis Reveals Sst2 as the Principal Regulator of Mating Pheromone Signaling in the Yeast Saccharomyces cerevisiae Eukaryot. Cell, February 1, 2006; 5(2): 330 - 346. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Trautwein, J. Dengjel, M. Schirle, and A. Spang Arf1p Provides an Unexpected Link between COPI Vesicles and mRNA in Saccharomyces cerevisiae Mol. Biol. Cell, November 1, 2004; 15(11): 5021 - 5037. [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]
|
|
|
|
|
|
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]
|
|
|
|
|
|
A.-M. Li, A. Watson, and J. L. Fridovich-Keil Scp160p associates with specific mRNAs in yeast Nucleic Acids Res., April 1, 2003; 31(7): 1830 - 1837. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. D. Lang, A.-m. Li, H. D. Black-Brewster, and J. L. Fridovich-Keil The brefeldin A resistance protein Bfr1p is a component of polyribosome-associated mRNP complexes in yeast Nucleic Acids Res., June 15, 2001; 29(12): 2567 - 2574. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. S. Cunningham, R. E. Dodson, M. A. Nagel, D. J. Shapiro, and D. R. Schoenberg Vigilin binding selectively inhibits cleavage of the vitellogenin mRNA 3'-untranslated region by the mRNA endonuclease polysomal ribonuclease 1 PNAS, October 23, 2000; (2000) 220425497. [Abstract] [Full Text]
|
|
|
|
|
|
S. Frey, M. Pool, and M. Seedorf Scp160p, an RNA-binding, Polysome-associated Protein, Localizes to the Endoplasmic Reticulum of Saccharomyces cerevisiae in a Microtubule-dependent Manner J. Biol. Chem., May 4, 2001; 276(19): 15905 - 15912. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. S. Cunningham, R. E. Dodson, M. A. Nagel, D. J. Shapiro, and D. R. Schoenberg Vigilin binding selectively inhibits cleavage of the vitellogenin mRNA 3'-untranslated region by the mRNA endonuclease polysomal ribonuclease 1 PNAS, November 7, 2000; 97(23): 12498 - 12502. [Abstract] [Full Text] [PDF]
|
|