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Tracking the evolution of a cold stress associated gene family in cold tolerant grasses.
BMC Evol Biol. 2008 Sep 05; 8:245.BE

Abstract

BACKGROUND

Grasses are adapted to a wide range of climatic conditions. Species of the subfamily Pooideae, which includes wheat, barley and important forage grasses, have evolved extreme frost tolerance. A class of ice binding proteins that inhibit ice re-crystallisation, specific to the Pooideae subfamily lineage, have been identified in perennial ryegrass and wheat, and these proteins are thought to have evolved from a leucine-rich repeat phytosulfokine receptor kinase (LRR-PSR)-like ancestor gene. Even though the ice re-crystallisation inhibition function of these proteins has been studied extensively in vitro, little is known about the evolution of these genes on the molecular level.

RESULTS

We identified 15 putative novel ice re-crystallisation inhibition (IRI)-like protein coding genes in perennial ryegrass, barley, and wheat. Using synonymous divergence estimates we reconstructed the evolution of the IRI-like gene family. We also explored the hypothesis that the IRI-domain has evolved through repeated motif expansion and investigated the evolutionary relationship between a LRR-domain containing IRI coding gene in carrot and the Pooideae IRI-like genes. Our analysis showed that the main expansion of the IRI-gene family happened ~36 million years ago (Mya). In addition to IRI-like paralogs, wheat contained several sequences that likely were products of polyploidisation events (homoeologs). Through sequence analysis we identified two short motifs in the rice LRR-PSR gene highly similar to the repeat motifs of the IRI-domain in cold tolerant grasses. Finally we show that the LRR-domain of carrot and grass IRI proteins both share homology to an Arabidopsis thaliana LRR-trans membrane protein kinase (LRR-TPK).

CONCLUSION

The diverse IRI-like genes identified in this study tell a tale of a complex evolutionary history including birth of an ice binding domain, a burst of gene duplication events after cold tolerant grasses radiated from rice, protein domain structure differentiation between paralogs, and sub- and/or neofunctionalisation of IRI-like proteins. From our sequence analysis we provide evidence for IRI-domain evolution probably occurring through increased copy number of a repeated motif. Finally, we discuss the possibility of parallel evolution of LRR domain containing IRI proteins in carrot and grasses through two completely different molecular adaptations.

Authors+Show Affiliations

Department of Plant and Environmental Sciences, University of Life Sciences, As, Norway. odd-simen.sandve@umb.noNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18775065

Citation

Sandve, Simen R., et al. "Tracking the Evolution of a Cold Stress Associated Gene Family in Cold Tolerant Grasses." BMC Evolutionary Biology, vol. 8, 2008, p. 245.
Sandve SR, Rudi H, Asp T, et al. Tracking the evolution of a cold stress associated gene family in cold tolerant grasses. BMC Evol Biol. 2008;8:245.
Sandve, S. R., Rudi, H., Asp, T., & Rognli, O. A. (2008). Tracking the evolution of a cold stress associated gene family in cold tolerant grasses. BMC Evolutionary Biology, 8, 245. https://doi.org/10.1186/1471-2148-8-245
Sandve SR, et al. Tracking the Evolution of a Cold Stress Associated Gene Family in Cold Tolerant Grasses. BMC Evol Biol. 2008 Sep 5;8:245. PubMed PMID: 18775065.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Tracking the evolution of a cold stress associated gene family in cold tolerant grasses. AU - Sandve,Simen R, AU - Rudi,Heidi, AU - Asp,Torben, AU - Rognli,Odd Arne, Y1 - 2008/09/05/ PY - 2008/04/30/received PY - 2008/09/05/accepted PY - 2008/9/9/pubmed PY - 2009/2/24/medline PY - 2008/9/9/entrez SP - 245 EP - 245 JF - BMC evolutionary biology JO - BMC Evol Biol VL - 8 N2 - BACKGROUND: Grasses are adapted to a wide range of climatic conditions. Species of the subfamily Pooideae, which includes wheat, barley and important forage grasses, have evolved extreme frost tolerance. A class of ice binding proteins that inhibit ice re-crystallisation, specific to the Pooideae subfamily lineage, have been identified in perennial ryegrass and wheat, and these proteins are thought to have evolved from a leucine-rich repeat phytosulfokine receptor kinase (LRR-PSR)-like ancestor gene. Even though the ice re-crystallisation inhibition function of these proteins has been studied extensively in vitro, little is known about the evolution of these genes on the molecular level. RESULTS: We identified 15 putative novel ice re-crystallisation inhibition (IRI)-like protein coding genes in perennial ryegrass, barley, and wheat. Using synonymous divergence estimates we reconstructed the evolution of the IRI-like gene family. We also explored the hypothesis that the IRI-domain has evolved through repeated motif expansion and investigated the evolutionary relationship between a LRR-domain containing IRI coding gene in carrot and the Pooideae IRI-like genes. Our analysis showed that the main expansion of the IRI-gene family happened ~36 million years ago (Mya). In addition to IRI-like paralogs, wheat contained several sequences that likely were products of polyploidisation events (homoeologs). Through sequence analysis we identified two short motifs in the rice LRR-PSR gene highly similar to the repeat motifs of the IRI-domain in cold tolerant grasses. Finally we show that the LRR-domain of carrot and grass IRI proteins both share homology to an Arabidopsis thaliana LRR-trans membrane protein kinase (LRR-TPK). CONCLUSION: The diverse IRI-like genes identified in this study tell a tale of a complex evolutionary history including birth of an ice binding domain, a burst of gene duplication events after cold tolerant grasses radiated from rice, protein domain structure differentiation between paralogs, and sub- and/or neofunctionalisation of IRI-like proteins. From our sequence analysis we provide evidence for IRI-domain evolution probably occurring through increased copy number of a repeated motif. Finally, we discuss the possibility of parallel evolution of LRR domain containing IRI proteins in carrot and grasses through two completely different molecular adaptations. SN - 1471-2148 UR - https://www.unboundmedicine.com/medline/citation/18775065/Tracking_the_evolution_of_a_cold_stress_associated_gene_family_in_cold_tolerant_grasses_ L2 - https://bmcevolbiol.biomedcentral.com/articles/10.1186/1471-2148-8-245 DB - PRIME DP - Unbound Medicine ER -