Stability of casein mRNA is ensured by structural interactions between the 3′-untranslated region and poly(A) tail via the HuR and poly(A)-binding protein complex

2006 ◽  
Vol 1759 (3-4) ◽  
pp. 132-140 ◽  
Author(s):  
Kentaro Nagaoka ◽  
Toshiyuki Suzuki ◽  
Tomomi Kawano ◽  
Kazuhiko Imakawa ◽  
Senkiti Sakai
Keyword(s):  
Protein Complex ◽  
Untranslated Region ◽  
Binding Protein ◽  
Structural Interactions

ASSOCIATION BEHAVIOUR OF THE OESTRADIOL-BINDING PROTEIN COMPLEX WITH THE NUCLEAR FRACTION

1972 ◽  
Vol 71 (2_Suppla) ◽  
pp. S420-S438 ◽  
Author(s):  
David L. Williams ◽  
Jack Gorski
Keyword(s):  
Binding Site ◽  
Protein Complex ◽  
Binding Protein ◽  
Nuclear Fraction ◽  
Site Saturation ◽  
Total Binding

ABSTRACT A number of studies have been carried out to examine the distribution of the oestradiol-binding protein complex between cytosol and nuclear fractions as a function of total binding site saturation. The results of these studies suggest that each binding protein has one binding site for the hormone. In addition, these studies suggest that the interaction of the oestradiol-binding protein complex with the nucleus involves a large number of low affinity association sites.

scholarly journals TbUNC119 and Its Binding Protein Complex Are Essential for Propagation, Motility, and Morphogenesis of Trypanosoma brucei Procyclic Form Cells

PLoS ONE ◽  
2010 ◽  
Vol 5 (12) ◽  
pp. e15577 ◽  
Author(s):  
Shigeru Ohshima ◽  
Mitsuko Ohashi-Suzuki ◽  
Yutaka Miura ◽  
Yoshisada Yabu ◽  
Noriko Okada ◽  
...  
Keyword(s):  
Trypanosoma Brucei ◽  
Protein Complex ◽  
Binding Protein ◽  
Procyclic Form

The Circulating Growth Hormone (GH)-Binding Protein Complex: A Major Constituent of Plasma GH in Man*

Endocrinology ◽  
1988 ◽  
Vol 122 (3) ◽  
pp. 976-984 ◽  
Author(s):  
GERHARD BAUMANN ◽  
KLAUS AMBURN ◽  
MELISSA A. SHAW
Keyword(s):  
Growth Hormone ◽  
Protein Complex ◽  
Binding Protein ◽  
Major Constituent ◽  
Plasma Gh

scholarly journals Involvement of the nuclear cap-binding protein complex in alternative splicing in Arabidopsis thaliana

2009 ◽  
Vol 38 (1) ◽  
pp. 265-278 ◽  
Author(s):  
Katarzyna Dorota Raczynska ◽  
Craig G. Simpson ◽  
Adam Ciesiolka ◽  
Lukasz Szewc ◽  
Dominika Lewandowska ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Alternative Splicing ◽  
Protein Complex ◽  
Binding Protein

scholarly journals Identification and characterization of a 44 kDa protein that binds specifically to the 3′-untranslated region of CYP2a5 mRNA: inducibility, subcellular distribution and possible role in mRNA stabilization

1996 ◽  
Vol 313 (3) ◽  
pp. 1029-1037 ◽  
Author(s):  
Olivier GENESTE ◽  
Françoise RAFFALLI ◽  
Matti A. LANG
Keyword(s):  
Half Life ◽  
Untranslated Region ◽  
Translational Regulation ◽  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Blocking Agent ◽  
Subcellular Fractionation ◽  
Mrna Stabilization ◽  
Nuclear Extracts

Stabilization of mRNA is important in the regulation of CYP2a5 expression but the factors involved in the process are not known [Aida and Negishi (1991) Biochemistry 30, 8041–8045]. In this paper, we describe, for the first time, a protein that binds specifically to the 3′-untranslated region of CYP2a5 mRNA and which is inducible by pyrazole, a compound known to increase the half-life of CYP2a5 mRNA. We also demonstrate that pyrazole treatment causes an elongation of the CYP2a5 mRNA poly(A) tail, and that phenobarbital, which is transcriptional activator of the CYP2a5 gene that does not affect the mRNA half-life, neither induces the RNA-binding protein nor affects the poly(A) tail size. SDS/PAGE of the UV-cross-linked RNA–protein complex demonstrated that the RNA-binding protein has an apparent molecular mass of 44 kDa. The protein-binding site was localized to a 70-nucleotide region between bases 1585 and 1655. Treatment of cytoplasmic extracts with an SH-oxidizing agent, diamide, an SH-blocking agent, N-ethylmaleimide or potato acid phosphatase abolished complex-formation, suggesting that the CYP2a5 mRNA-binding protein is subject to post-translational regulation. Subcellular fractionation showed that the 44 kDa protein is present in polyribosomes and nuclei, and that its apparent induction is much stronger in polyribosomes than in nuclear extracts. We propose that this 44 kDA RNA-binding protein is involved in the stabilization of CYP2a5 mRNA by controlling the length of the poly(A) tail.

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