The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein

doi:10.1083/jcb.96.3.717

This Article

	Full Text (PDF, 871K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JCB
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Baer, B. W.
	Articles by Kornberg, R. D.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Baer, B. W.
	Articles by Kornberg, R. D.


Social Bookmarking

	What's this?

ARTICLES

The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein

BW Baer and RD Kornberg

A 75,000-dalton protein has been purified approximately 1,000-fold from rat liver, based on its capacity to organize poly(A) in a 27-residue repeating structure. This protein may be identified with the major polypeptide component of cytoplasmic poly(A)-ribonucleoprotein (RNP) previously described. The poly(A)-organizing activity of the protein is detected only in cytoplasmic fractions. Upon nuclease digestion of the 75,000-dalton protein-poly(A) complex, monomers, and higher multimers of RNP subunits can be resolved in a sucrose gradient. The sedimentation rate of the monomer is compatible with a composition of one 75,000-dalton protein molecule and one 27-residue segment of poly(A).
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Schwede, A., Manful, T., Jha, B. A., Helbig, C., Bercovich, N., Stewart, M., Clayton, C. (2009). The role of deadenylation in the degradation of unstable mRNAs in trypanosomes. Nucleic Acids Res 37: 5511-5528 [Abstract] [Full Text]
Polacek, C., Friebe, P., Harris, E. (2009). Poly(A)-binding protein binds to the non-polyadenylated 3' untranslated region of dengue virus and modulates translation efficiency. J. Gen. Virol. 90: 687-692 [Abstract] [Full Text]
Viphakone, N., Voisinet-Hakil, F., Minvielle-Sebastia, L. (2008). Molecular dissection of mRNA poly(A) tail length control in yeast. Nucleic Acids Res 36: 2418-2433 [Abstract] [Full Text]
Littauer, U. Z. (2005). From Polynucleotide Phosphorylase to Neurobiology. J. Biol. Chem. 280: 38889-38897 [Full Text]
Matsumoto, K., Tanaka, K. J., Tsujimoto, M. (2005). An Acidic Protein, YBAP1, Mediates the Release of YB-1 from mRNA and Relieves the Translational Repression Activity of YB-1. Mol. Cell. Biol. 25: 1779-1792 [Abstract] [Full Text]
DOWER, K., KUPERWASSER, N., MERRIKH, H., ROSBASH, M. (2004). A synthetic A tail rescues yeast nuclear accumulation of a ribozyme-terminated transcript. RNA 10: 1888-1899 [Abstract] [Full Text]
Mangus, D. A., Evans, M. C., Agrin, N. S., Smith, M., Gongidi, P., Jacobson, A. (2004). Positive and Negative Regulation of Poly(A) Nuclease. Mol. Cell. Biol. 24: 5521-5533 [Abstract] [Full Text]
Kuyumcu-Martinez, N. M., Joachims, M., Lloyd, R. E. (2002). Efficient Cleavage of Ribosome-Associated Poly(A)-Binding Protein by Enterovirus 3C Protease. J. Virol. 76: 2062-2074 [Abstract] [Full Text]
Khaleghpour, K., Kahvejian, A., De Crescenzo, G., Roy, G., Svitkin, Y. V., Imataka, H., O'Connor-McCourt, M., Sonenberg, N. (2001). Dual Interactions of the Translational Repressor Paip2 with Poly(A) Binding Protein. Mol. Cell. Biol. 21: 5200-5213 [Abstract] [Full Text]
Knight, J. E., Narus, E. N., Martin, S. L., Jacobson, A., Barnes, B. M., Boyer, B. B. (2000). mRNA Stability and Polysome Loss in Hibernating Arctic Ground Squirrels (Spermophilus parryii). Mol. Cell. Biol. 20: 6374-6379 [Abstract] [Full Text]
Theodorakis, N. G., de Maio, A. (1999). Cx32 mRNA in rat liver: effects of inflammation on poly(A) tail distribution and mRNA degradation. Am. J. Physiol. Regul. Integr. Comp. Physiol. 276: R1249-R1257 [Abstract] [Full Text]
Kerekatte, V., Keiper, B. D., Badorff, C., Cai, A., Knowlton, K. U., Rhoads, R. E. (1999). Cleavage of Poly(A)-Binding Protein by Coxsackievirus 2A Protease In Vitro and In Vivo: Another Mechanism for Host Protein Synthesis Shutoff?. J. Virol. 73: 709-717 [Abstract] [Full Text]
Joachims, M., Van Breugel, P. C., Lloyd, R. E. (1999). Cleavage of Poly(A)-Binding Protein by Enterovirus Proteases Concurrent with Inhibition of Translation In Vitro. J. Virol. 73: 718-727 [Abstract] [Full Text]
Mangus, D. A., Amrani, N., Jacobson, A. (1998). Pbp1p, a Factor Interacting with Saccharomyces cerevisiae Poly(A)-Binding Protein, Regulates Polyadenylation. Mol. Cell. Biol. 18: 7383-7396 [Abstract] [Full Text]
Russell, J. E., Morales, J., Makeyev, A. V., Liebhaber, S. A. (1998). Sequence Divergence in the 3' Untranslated Regions of Human zeta - and alpha -Globin mRNAs Mediates a Difference in Their Stabilities and Contributes to Efficient alpha -to-zeta Gene Developmental Switching. Mol. Cell. Biol. 18: 2173-2183 [Abstract] [Full Text]
Staton, J. M., Leedman, P. J. (1998). Posttranscriptional Regulation of Thyrotropin {beta}-Subunit Messenger Ribonucleic Acid by Thyroid Hormone in Murine Thyrotrope Tumor Cells: A Conserved Mechanism across Species. Endocrinology 139: 1093-1100 [Abstract] [Full Text]
Couttet, P., Fromont-Racine, M., Steel, D., Pictet, R., Grange, T. (1997). Messenger RNA deadenylylation precedes decapping in mammalian�cells. Proc. Natl. Acad. Sci. USA 94: 5628-5633 [Abstract] [Full Text]
Korner, C. G., Wahle, E. (1997). Poly(A) Tail Shortening by a Mammalian Poly(A)-specific 3'-Exoribonuclease. J. Biol. Chem. 272: 10448-10456 [Abstract] [Full Text]
Proweller, A., Butler, J. S. (1996). Ribosomal Association of Poly(A)-binding Protein in Poly(A)-deficient Saccharomyces cerevisiae. J. Biol. Chem. 271: 10859-10865 [Abstract] [Full Text]
Thisted, T., Lyakhov, D. L., Liebhaber, S. A. (2001). Optimized RNA Targets of Two Closely Related Triple KH Domain Proteins, Heterogeneous Nuclear Ribonucleoprotein K and alpha CP-2KL, Suggest Distinct Modes of RNA Recognition. J. Biol. Chem. 276: 17484-17496 [Abstract] [Full Text]