Skip to main content
Journal cover image

Rapid evolution in plant chitinases: molecular targets of selection in plant-pathogen coevolution.

Publication ,  Conference
Bishop, JG; Dean, AM; Mitchell-Olds, T
Published in: Proceedings of the National Academy of Sciences of the United States of America
May 2000

Many pathogen recognition genes, such as plant R-genes, undergo rapid adaptive evolution, providing evidence that these genes play a critical role in plant-pathogen coevolution. Surprisingly, whether rapid adaptive evolution also occurs in genes encoding other kinds of plant defense proteins is unknown. Unlike recognition proteins, plant chitinases attack pathogens directly, conferring disease resistance by degrading chitin, a component of fungal cell walls. Here, we show that nonsynonymous substitution rates in plant class I chitinase often exceed synonymous rates in the plant genus Arabis (Cruciferae) and in other dicots, indicating a succession of adaptively driven amino acid replacements. We identify individual residues that are likely subject to positive selection by using codon substitution models and determine the location of these residues on the three-dimensional structure of class I chitinase. In contrast to primate lysozymes and plant class III chitinases, structural and functional relatives of class I chitinase, the adaptive replacements of class I chitinase occur disproportionately in the active site cleft. This highly unusual pattern of replacements suggests that fungi directly defend against chitinolytic activity through enzymatic inhibition or other forms of chemical resistance and identifies target residues for manipulating chitinolytic activity. These data also provide empirical evidence that plant defense proteins not involved in pathogen recognition also evolve in a manner consistent with rapid coevolutionary interactions.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

Proceedings of the National Academy of Sciences of the United States of America

DOI

EISSN

1091-6490

ISSN

0027-8424

Publication Date

May 2000

Volume

97

Issue

10

Start / End Page

5322 / 5327

Related Subject Headings

  • Protein Conformation
  • Plant Diseases
  • Phylogeny
  • Molecular Sequence Data
  • Models, Molecular
  • Evolution, Molecular
  • Conserved Sequence
  • Chitinases
  • Brassicaceae
  • Brassica
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Bishop, J. G., Dean, A. M., & Mitchell-Olds, T. (2000). Rapid evolution in plant chitinases: molecular targets of selection in plant-pathogen coevolution. In Proceedings of the National Academy of Sciences of the United States of America (Vol. 97, pp. 5322–5327). https://doi.org/10.1073/pnas.97.10.5322
Bishop, J. G., A. M. Dean, and T. Mitchell-Olds. “Rapid evolution in plant chitinases: molecular targets of selection in plant-pathogen coevolution.” In Proceedings of the National Academy of Sciences of the United States of America, 97:5322–27, 2000. https://doi.org/10.1073/pnas.97.10.5322.
Bishop JG, Dean AM, Mitchell-Olds T. Rapid evolution in plant chitinases: molecular targets of selection in plant-pathogen coevolution. In: Proceedings of the National Academy of Sciences of the United States of America. 2000. p. 5322–7.
Bishop, J. G., et al. “Rapid evolution in plant chitinases: molecular targets of selection in plant-pathogen coevolution.Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 10, 2000, pp. 5322–27. Epmc, doi:10.1073/pnas.97.10.5322.
Bishop JG, Dean AM, Mitchell-Olds T. Rapid evolution in plant chitinases: molecular targets of selection in plant-pathogen coevolution. Proceedings of the National Academy of Sciences of the United States of America. 2000. p. 5322–5327.
Journal cover image

Published In

Proceedings of the National Academy of Sciences of the United States of America

DOI

EISSN

1091-6490

ISSN

0027-8424

Publication Date

May 2000

Volume

97

Issue

10

Start / End Page

5322 / 5327

Related Subject Headings

  • Protein Conformation
  • Plant Diseases
  • Phylogeny
  • Molecular Sequence Data
  • Models, Molecular
  • Evolution, Molecular
  • Conserved Sequence
  • Chitinases
  • Brassicaceae
  • Brassica