| Accelerated evolution and coevolution drove the evolutionary history of AGPase sub-units during angiosperm radiation. | |
| | |
MedLine Citation:
|
PMID: 22307567 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
BACKGROUND AND AIMS: ADP-glucose pyrophosphorylase (AGPase) is a key enzyme of starch biosynthesis. In the green plant lineage, it is composed of two large (LSU) and two small (SSU) sub-units encoded by paralogous genes, as a consequence of several rounds of duplication. First, our aim was to detect specific patterns of molecular evolution following duplication events and the divergence between monocotyledons and dicotyledons. Secondly, we investigated coevolution between amino acids both within and between sub-units. METHODS: A phylogeny of each AGPase sub-unit was built using all gymnosperm and angiosperm sequences available in databases. Accelerated evolution along specific branches was tested using the ratio of the non-synonymous to the synonymous substitution rate. Coevolution between amino acids was investigated taking into account compensatory changes between co-substitutions. KEY RESULTS: We showed that SSU paralogues evolved under high functional constraints during angiosperm radiation, with a significant level of coevolution between amino acids that participate in SSU major functions. In contrast, in the LSU paralogues, we identified residues under positive selection (1) following the first LSU duplication that gave rise to two paralogues mainly expressed in angiosperm source and sink tissues, respectively; and (2) following the emergence of grass-specific paralogues expressed in the endosperm. Finally, we found coevolution between residues that belong to the interaction domains of both sub-units. CONCLUSIONS: Our results support the view that coevolution among amino acid residues, especially those lying in the interaction domain of each sub-unit, played an important role in AGPase evolution. First, within SSU, coevolution allowed compensating mutations in a highly constrained context. Secondly, the LSU paralogues probably acquired tissue-specific expression and regulatory properties via the coevolution between sub-unit interacting domains. Finally, the pattern we observed during LSU evolution is consistent with repeated sub-functionalization under 'Escape from Adaptive Conflict', a model rarely illustrated in the literature. |
| | |
Authors:
|
Jonathan Corbi; Julien Y Dutheil; Catherine Damerval; Maud I Tenaillon; Domenica Manicacci |
Related Documents
:
|
22407317 - Structure and mechanism of a glutamate-gaba antiporter. 11677837 - Action mechanism of betahistine in the vestibular end organs. 8960397 - Selective reduction in domoic acid toxicity in vivo by a novel non-n-methyl-d-aspartate... 7108527 - Effects of kainic acid on high-energy metabolites in the mouse striatum. 6146187 - Adrenergic receptors and gastric secretion in dogs. is a "tonic balance" relationship b... 7335107 - Potentiation of genotoxicity by concurrent application of compounds found in betel quid... |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2012-02-02 |
Journal Detail:
|
Title: Annals of botany Volume: 109 ISSN: 1095-8290 ISO Abbreviation: Ann. Bot. Publication Date: 2012 Mar |
Date Detail:
|
Created Date: 2012-02-27 Completed Date: 2012-09-06 Revised Date: 2013-05-20 |
Medline Journal Info:
|
Nlm Unique ID: 0372347 Medline TA: Ann Bot Country: England |
Other Details:
|
Languages: eng Pagination: 693-708 Citation Subset: IM |
Affiliation:
|
CNRS, UMR Génétique Végétale, Gif sur Yvette, France. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Amino Acid Sequence Angiosperms / enzymology, genetics*, radiation effects* Base Sequence Evolution, Molecular* Gene Duplication Gene Expression Regulation, Plant Genes, Plant Genetic Variation Glucose-1-Phosphate Adenylyltransferase / metabolism* Molecular Sequence Data Phylogeny Selection, Genetic Starch / biosynthesis |
| Chemical | |
Reg. No./Substance:
|
9005-25-8/Starch; EC 2.7.7.27/Glucose-1-Phosphate Adenylyltransferase |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Soy isoflavone supplementation for breast cancer risk reduction: a randomized phase II trial.
Next Document: Virus-induced gene silencing (VIGS) in Cysticapnos vesicaria, a zygomorphic-flowered Papaveraceae (R...