MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yu, J.
Right arrow Articles by Russell, J. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yu, J.
Right arrow Articles by Russell, J. E.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, September 2001, p. 5879-5888, Vol. 21, No. 17
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.17.5879-5888.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Structural and Functional Analysis of an mRNP Complex That Mediates the High Stability of Human beta -Globin mRNA

Jia Yu1 and J. Eric Russell1,2,*

Departments of Medicine1 (Hematology/Oncology) and Pediatrics (Hematology),2 University of Pennsylvania School of Medicine and The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104

Received 12 April 2001/Returned for modification 10 May 2001/Accepted 7 June 2001

Human globins are encoded by mRNAs exhibiting high stabilities in transcriptionally silenced erythrocyte progenitors. Unlike alpha -globin mRNA, whose stability is enhanced by assembly of a specific messenger RNP (mRNP) alpha  complex on its 3' untranslated region (UTR), neither the structure(s) nor the mechanism(s) that effects the high-level stability of human beta -globin mRNA has been identified. The present work describes an mRNP complex assembling on the 3' UTR of the beta -globin mRNA that exhibits many of the properties of the stability-enhancing alpha  complex. The beta -globin mRNP complex is shown to contain one or more factors homologous to alpha CP, a 39-kDa RNA-binding protein that is integral to alpha -complex assembly. Sequence analysis implicates a specific 14-nucleotide pyrimidine-rich track within its 3' UTR as the site of beta -globin mRNP assembly. The importance of this track to mRNA stability is subsequently verified in vivo using mice expressing human beta -globin transgenes that contain informative mutations in this region. In combination, the in vitro and in vivo analyses indicate that the high stabilities of the alpha - and beta -globin mRNAs are maintained through related mRNP complexes that may share a common regulatory pathway.

* Corresponding author. Mailing address: Abramson Research Building, Room 316F, The Children's Hospital of Philadelphia, 34th St. and Civic Center Blvd., Philadelphia, PA 19104. Phone: (215) 590-3880. Fax: (215) 590-4834. E-mail: jeruss{at}mail.med.upenn.edu.

Molecular and Cellular Biology, September 2001, p. 5879-5888, Vol. 21, No. 17
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.17.5879-5888.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2001 by the American Society for Microbiology. All rights reserved.