Plant Cell email content delivery
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 ISI Web of Science (89)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Werneke, J. M.
Right arrow Articles by Ogren, W. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Werneke, J. M.
Right arrow Articles by Ogren, W. L.
Agricola
Right arrow Articles by Werneke, J. M.
Right arrow Articles by Ogren, W. L.

THE PLANT CELL, Vol 1, Issue 8 815-825, Copyright © 1989 by American Society of Plant Biologists

RESEARCH ARTICLES

Alternative mRNA Splicing Generates the Two Ribulosebisphosphate Carboxylase/Oxygenase Activase Polypeptides in Spinach and Arabidopsis

J. M. Werneke, J. M. Chatfield and W. L. Ogren
Agricultural Research Service, United States Department of Agriculture, 1102 South Goodwin Avenue, Urbana, Illinois 61801

Sequence analysis of ribulosebisphosphate carboxylase/oxygenase (rubisco) activase cDNA and genomic clones isolated from spinach and Arabidopsis thaliana indicates that the two polypeptides of rubisco activase arise from alternative splicing of a common pre-mRNA. In spinach, two 5[prime] splice sites are used in processing a single 137-nucleotide intron near the 3[prime] end of the primary transcript. This intron was either removed completely or, alternatively, the first 22 nucleotides of the intervening sequence were retained in the mature rubisco activase mRNA. The 22-nucleotide auxiliary exon contains an in-frame ochre termination codon and leads to the synthesis of a 41-kilodalton polypeptide. Removal of the entire 137-nucleotide intervening sequence results in the synthesis of a larger 45-kilodalton polypeptide. Thus, alternative splicing of the spinach rubisco activase mRNA results in the synthesis of two polypeptides that are identical except for 37 additional amino acids at the C terminus of the 45-kilodalton polypeptide. This conclusion was confirmed by Cleveland peptide mapping and by N-terminal and C-terminal amino acid sequence analyses of both purified polypeptides. This method of producing the two rubisco activase polypeptides may be an evolutionarily conserved feature in higher plants because a nearly identical process occurs in the production of the two rubisco activase polypeptides in Arabidopsis. In Arabidopsis, an alternatively spliced intron resides at precisely the same position as the alternatively spliced intron in spinach and results in the synthesis of 44-kilodalton and 47-kilodalton rubisco activase polypeptides. In contrast to spinach, however, the retained portion of the intervening sequence does not contain an in-frame termination codon. Rather, a shift in reading frame leads to termination of translation of the smaller polypeptide within the coding region of the larger polypeptide.


This article has been cited by other articles:


Home page
 Genome ResHome page
W. B. Barbazuk, Y. Fu, and K. M. McGinnis
Genome-wide analyses of alternative splicing in plants: Opportunities and challenges
Genome Res., September 1, 2008; 18(9): 1381 - 1392.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
M. A. J. Parry, A. J. Keys, P. J. Madgwick, A. E. Carmo-Silva, and P. J. Andralojc
Rubisco regulation: a role for inhibitors
J. Exp. Bot., May 1, 2008; 59(7): 1569 - 1580.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
A. Prins, P. D.R. van Heerden, E. Olmos, K. J. Kunert, and C. H. Foyer
Cysteine proteinases regulate chloroplast protein content and composition in tobacco leaves: a model for dynamic interactions with ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) vesicular bodies
J. Exp. Bot., May 1, 2008; 59(7): 1935 - 1950.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
I. Kurek, T. K. Chang, S. M. Bertain, A. Madrigal, L. Liu, M. W. Lassner, and G. Zhu
Enhanced Thermostability of Arabidopsis Rubisco Activase Improves Photosynthesis and Growth Rates under Moderate Heat Stress
PLANT CELL, October 1, 2007; 19(10): 3230 - 3241.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Bot.Home page
D. J. Weston, W. L. Bauerle, G. A. Swire-Clark, B. d. Moore, and Wm. V. Baird
Characterization of Rubisco activase from thermally contrasting genotypes of Acer rubrum (Aceraceae)
Am. J. Botany, June 1, 2007; 94(6): 926 - 934.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. Wang and A. R. Portis Jr.
Increased Sensitivity of Oxidized Large Isoform of Ribulose-1,5-bisphosphate Carboxylase/Oxygenase (Rubisco) Activase to ADP Inhibition Is Due to an Interaction between Its Carboxyl Extension and Nucleotide-binding Pocket
J. Biol. Chem., September 1, 2006; 281(35): 25241 - 25249.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
B.-B. Wang and V. Brendel
Genomewide comparative analysis of alternative splicing in plants
PNAS, May 2, 2006; 103(18): 7175 - 7180.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
M. Vargas-Suarez, A. Ayala-Ochoa, J. Lozano-Franco, I. Garcia-Torres, A. Diaz-Quinonez, V. F. Ortiz-Navarrete, and E. Sanchez-de-Jimenez
Rubisco activase chaperone activity is regulated by a post-translational mechanism in maize leaves
J. Exp. Bot., December 1, 2004; 55(408): 2533 - 2539.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
M. Bey, K. Stuber, K. Fellenberg, Z. Schwarz-Sommer, H. Sommer, H. Saedler, and S. Zachgo
Characterization of Antirrhinum Petal Development and Identification of Target Genes of the Class B MADS Box Gene DEFICIENS
PLANT CELL, December 1, 2004; 16(12): 3197 - 3215.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. Johansson, O. Olsson, and T. Nystrom
Progression and Specificity of Protein Oxidation in the Life Cycle of Arabidopsis thaliana
J. Biol. Chem., May 21, 2004; 279(21): 22204 - 22208.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
R. S. McKibbin, M. D. Wilkinson, P. C. Bailey, J. E. Flintham, L. M. Andrew, P. A. Lazzeri, M. D. Gale, J. R. Lenton, and M. J. Holdsworth
Transcripts of Vp-1 homeologues are misspliced in modern wheat and ancestral species
PNAS, July 23, 2002; 99(15): 10203 - 10208.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
S. Shigeoka, T. Ishikawa, M. Tamoi, Y. Miyagawa, T. Takeda, Y. Yabuta, and K. Yoshimura
Regulation and function of ascorbate peroxidase isoenzymes
J. Exp. Bot., May 15, 2002; 53(372): 1305 - 1319.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
N. A. Eckardt
Alternative Splicing and the Control of Flowering Time
PLANT CELL, April 1, 2002; 14(4): 743 - 747.
[Full Text] [PDF]

Home page
 Plant Physiol.Home page
R. P. Kallis, R. G. Ewy, and A. R. Portis Jr.
Alteration of the Adenine Nucleotide Response and Increased Rubisco Activation Activity of Arabidopsis Rubisco Activase by Site-Directed Mutagenesis
Plant Physiology, July 1, 2000; 123(3): 1077 - 1086.
[Abstract] [Full Text]

Home page
 Proc. Natl. Acad. Sci. USAHome page
N. Zhang and A. R. Portis Jr.
Mechanism of light regulation of Rubisco: A specific role for the larger Rubisco activase isoform involving reductive activation by thioredoxin-f
PNAS, August 3, 1999; 96(16): 9438 - 9443.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
P. A. Okubara, K. Pawlowski, T. M. Murphy, and A. M. Berry
Symbiotic Root Nodules of the Actinorhizal Plant Datisca glomerata Express Rubisco Activase mRNA
Plant Physiology, June 1, 1999; 120(2): 411 - 420.
[Abstract] [Full Text]

Home page
 Genes Dev.Home page
S. Lopato, M. Kalyna, S. Dorner, R. Kobayashi, A. R. Krainer, and A. Barta
atSRp30, one of two SF2/ASF-like proteins from Arabidopsis thaliana, regulates splicing of specific plant genes
Genes & Dev., April 15, 1999; 13(8): 987 - 1001.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications THE PLANT CELL PLANT PHYSIOLOGY
Copyright © 1989 by the American Society of Plant Biologists