@ARTICLE{TreeBASE2Ref20631,
author = {Paul H. Goodwin and Weilong Xie and Moez Valliani},
title = {Three genes of miraculin-like proteins from Nicotiana benthamiana with dissimilar putative structures show highly similar patterns of induction following bacterial and fungal infections},
year = {2012},
keywords = {Colletotrichum destructivum, Colletotrichum orbiculare, Hemibiotrophy, Hypersensitive response, Pseudomonas syringae pv. tabaci, Serine proteinase inhibitor},
doi = {10.1007/s10658-012-0056-8},
url = {http://www.springerlink.com/content/15247104926521g4/},
pmid = {},
journal = {European Journal of Plant Pathology},
volume = {134},
number = {4},
pages = {795--810},
abstract = {Expression of three Nicotiana benthamiana miraculin-like protein genes, NbMLP1, NbMLP2 and NbMLP3, showed almost identical responses to wounding, an incompatible interaction with Pseudomonas syringae pv. tabaci and compatible interactions with P. syringae pv. tabaci, Colletotrichum destructivum or Colletotrichum orbiculare. However, only NbMLP1 expression responded to methyl jasmonate and ethylene. None exhibited expression in healthy leaves and stems, and all showed highest expression in seeds, except for NbMLP1, which had highest expression in roots. NbMLP1, NbMLP2 and NbMLP3 were in different subfamilies of miraculin-like protein sequences of N. benthamiana and Nicotiana tabacum. Subfamilies correlated well with predicted features of the reactive-site loop potentially affecting the bond that could react with serine proteinases. Despite considerable predicted structural diversity that might affect biological activity, the apparently coordinated expression of these genes to pathogen attack may reflect the need to produce diverse proteinase inhibitors to act against a potentially broad range of secreted microbial proteinases during basal resistance to pathogens.}
}
Citation for Study 12626
Citation title:
"Three genes of miraculin-like proteins from Nicotiana benthamiana with dissimilar putative structures show highly similar patterns of induction following bacterial and fungal infections".
Study name:
"Three genes of miraculin-like proteins from Nicotiana benthamiana with dissimilar putative structures show highly similar patterns of induction following bacterial and fungal infections".
This study is part of submission 12626
(Status: Published).
Citation
Goodwin P., Xie W., & Valliani M. 2012. Three genes of miraculin-like proteins from Nicotiana benthamiana with dissimilar putative structures show highly similar patterns of induction following bacterial and fungal infections. European Journal of Plant Pathology, 134(4): 795-810.
Authors
-
Goodwin P.
-
Xie W.
-
Valliani M.
(submitter)
519-824-4120 x58110
Abstract
Expression of three Nicotiana benthamiana miraculin-like protein genes, NbMLP1, NbMLP2 and NbMLP3, showed almost identical responses to wounding, an incompatible interaction with Pseudomonas syringae pv. tabaci and compatible interactions with P. syringae pv. tabaci, Colletotrichum destructivum or Colletotrichum orbiculare. However, only NbMLP1 expression responded to methyl jasmonate and ethylene. None exhibited expression in healthy leaves and stems, and all showed highest expression in seeds, except for NbMLP1, which had highest expression in roots. NbMLP1, NbMLP2 and NbMLP3 were in different subfamilies of miraculin-like protein sequences of N. benthamiana and Nicotiana tabacum. Subfamilies correlated well with predicted features of the reactive-site loop potentially affecting the bond that could react with serine proteinases. Despite considerable predicted structural diversity that might affect biological activity, the apparently coordinated expression of these genes to pathogen attack may reflect the need to produce diverse proteinase inhibitors to act against a potentially broad range of secreted microbial proteinases during basal resistance to pathogens.
Keywords
Colletotrichum destructivum, Colletotrichum orbiculare, Hemibiotrophy, Hypersensitive response, Pseudomonas syringae pv. tabaci, Serine proteinase inhibitor
External links
About this resource
- Canonical resource URI:
http://purl.org/phylo/treebase/phylows/study/TB2:S12626
- Other versions:
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- Show BibTeX reference
@ARTICLE{TreeBASE2Ref20631,
author = {Paul H. Goodwin and Weilong Xie and Moez Valliani},
title = {Three genes of miraculin-like proteins from Nicotiana benthamiana with dissimilar putative structures show highly similar patterns of induction following bacterial and fungal infections},
year = {2012},
keywords = {Colletotrichum destructivum, Colletotrichum orbiculare, Hemibiotrophy, Hypersensitive response, Pseudomonas syringae pv. tabaci, Serine proteinase inhibitor},
doi = {10.1007/s10658-012-0056-8},
url = {http://www.springerlink.com/content/15247104926521g4/},
pmid = {},
journal = {European Journal of Plant Pathology},
volume = {134},
number = {4},
pages = {795--810},
abstract = {Expression of three Nicotiana benthamiana miraculin-like protein genes, NbMLP1, NbMLP2 and NbMLP3, showed almost identical responses to wounding, an incompatible interaction with Pseudomonas syringae pv. tabaci and compatible interactions with P. syringae pv. tabaci, Colletotrichum destructivum or Colletotrichum orbiculare. However, only NbMLP1 expression responded to methyl jasmonate and ethylene. None exhibited expression in healthy leaves and stems, and all showed highest expression in seeds, except for NbMLP1, which had highest expression in roots. NbMLP1, NbMLP2 and NbMLP3 were in different subfamilies of miraculin-like protein sequences of N. benthamiana and Nicotiana tabacum. Subfamilies correlated well with predicted features of the reactive-site loop potentially affecting the bond that could react with serine proteinases. Despite considerable predicted structural diversity that might affect biological activity, the apparently coordinated expression of these genes to pathogen attack may reflect the need to produce diverse proteinase inhibitors to act against a potentially broad range of secreted microbial proteinases during basal resistance to pathogens.}
}
- Show RIS reference
TY - JOUR
ID - 20631
AU - Goodwin,Paul H.
AU - Xie,Weilong
AU - Valliani,Moez
T1 - Three genes of miraculin-like proteins from Nicotiana benthamiana with dissimilar putative structures show highly similar patterns of induction following bacterial and fungal infections
PY - 2012
KW - Colletotrichum destructivum
KW - Colletotrichum orbiculare
KW - Hemibiotrophy
KW - Hypersensitive response
KW - Pseudomonas syringae pv. tabaci
KW - Serine proteinase inhibitor
UR - http://www.springerlink.com/content/15247104926521g4/
N2 - Expression of three Nicotiana benthamiana miraculin-like protein genes, NbMLP1, NbMLP2 and NbMLP3, showed almost identical responses to wounding, an incompatible interaction with Pseudomonas syringae pv. tabaci and compatible interactions with P. syringae pv. tabaci, Colletotrichum destructivum or Colletotrichum orbiculare. However, only NbMLP1 expression responded to methyl jasmonate and ethylene. None exhibited expression in healthy leaves and stems, and all showed highest expression in seeds, except for NbMLP1, which had highest expression in roots. NbMLP1, NbMLP2 and NbMLP3 were in different subfamilies of miraculin-like protein sequences of N. benthamiana and Nicotiana tabacum. Subfamilies correlated well with predicted features of the reactive-site loop potentially affecting the bond that could react with serine proteinases. Despite considerable predicted structural diversity that might affect biological activity, the apparently coordinated expression of these genes to pathogen attack may reflect the need to produce diverse proteinase inhibitors to act against a potentially broad range of secreted microbial proteinases during basal resistance to pathogens.
L3 - 10.1007/s10658-012-0056-8
JF - European Journal of Plant Pathology
VL - 134
IS - 4
SP - 795
EP - 810
ER -
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