Plant Physiol. Tips for Better Browsing
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
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 Email this article to a friend
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hilson, P.
Right arrow Articles by Masson, P. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hilson, P.
Right arrow Articles by Masson, P. H.
Agricola
Right arrow Articles by Hilson, P.
Right arrow Articles by Masson, P. H.

PLANT PHYSIOLOGY , Vol 103, Issue 2 525-533, Copyright © 1993 by American Society of Plant Biologists


MOLECULAR BIOLOGY AND GENE REGULATION

Molecular Characterization of PAB2, a Member of the Multigene Family Coding for Poly(A)-Binding Proteins in Arabidopsis thaliana

P. Hilson, K. L. Carroll and P. H. Masson
Laboratory of Genetics, University of Wisconsin, Madison, Wisconsin 53706 (P.H., K.L.C., P.H.M.);

The poly(A) tail of eukaryotic mRNAs associates with poly(A)-binding (PAB) proteins whose role in mRNA translation and stability is being intensively investigated. Very little is known about the structure and function of the PAB genes in plants. We have cloned multiple PAB-related sequences from Arabidopsis thaliana. Results suggest that PAB proteins are encoded by a multigene family. One member of this family (PAB2) is expressed in root and shoot tissues. The complete nucleotide sequence of PAB2 was determined. Study of the predicted PAB2 protein reveals a similarity in structure among vertebrate, insect, yeast, and plant PAB proteins. All contain two highly conserved domains: an amino-terminal sequence formed by four RNA recognition motifs and an uncharacterized carboxyl-terminal region of 69 to 71 amino acids. Possible roles for the carboxyl-terminal conserved domain are discussed in view of recently published data concerning the structure and function of PAB proteins.


This article has been cited by other articles:


Home page
Plant Physiol.Home page
L. Yuan, D. Loque, F. Ye, W. B. Frommer, and N. von Wiren
Nitrogen-Dependent Posttranscriptional Regulation of the Ammonium Transporter AtAMT1;1
Plant Physiology, February 1, 2007; 143(2): 732 - 744.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
Z. J. Lorkovic and A. Barta
Genome analysis: RNA recognition motif (RRM) and K homology (KH) domain RNA-binding proteins from the flowering plant Arabidopsis thaliana
Nucleic Acids Res., February 1, 2002; 30(3): 623 - 635.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
C. B. Yohn, A. Cohen, A. Danon, and S. P. Mayfield
A poly(A) binding protein functions in the chloroplast as a message-specific translation factor
PNAS, March 3, 1998; 95(5): 2238 - 2243.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1993 by the American Society of Plant Biologists