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Comparative Analysis of Zinc Finger Proteins Involved in Plant Disease Resistance

A meta-analysis was performed to understand the role of zinc finger domains in proteins of resistance (R) genes cloned from different crops. We analyzed protein sequences of seventy R genes of various crops in which twenty six proteins were found to have zinc finger domains along with nucleotide bin...

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Autores principales: Gupta, Santosh Kumar, Rai, Amit Kumar, Kanwar, Shamsher Singh, Sharma, Tilak R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2012
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3419713/
https://www.ncbi.nlm.nih.gov/pubmed/22916136
http://dx.doi.org/10.1371/journal.pone.0042578
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author Gupta, Santosh Kumar
Rai, Amit Kumar
Kanwar, Shamsher Singh
Sharma, Tilak R.
author_facet Gupta, Santosh Kumar
Rai, Amit Kumar
Kanwar, Shamsher Singh
Sharma, Tilak R.
author_sort Gupta, Santosh Kumar
collection PubMed
description A meta-analysis was performed to understand the role of zinc finger domains in proteins of resistance (R) genes cloned from different crops. We analyzed protein sequences of seventy R genes of various crops in which twenty six proteins were found to have zinc finger domains along with nucleotide binding sites - leucine rice repeats (NBS-LRR) domains. We identified thirty four zinc finger domains in the R proteins of nine crops and were grouped into 19 types of zinc fingers. The size of individual zinc finger domain within the R genes varied from 11 to 84 amino acids, whereas the size of proteins containing these domains varied from 263 to 1305 amino acids. The biophysical analysis revealed that molecular weight of Pi54 zinc finger was lowest whereas the highest one was found in rice Pib zinc finger named as Transposes Transcription Factor (TTF). The instability (R(2) = 0.95) and the aliphatic (R(2) = 0.94) indices profile of zinc finger domains follows the polynomial distribution pattern. The pairwise identity analysis showed that the Lin11, Isl-1 & Mec-3 (LIM) zinc finger domain of rice blast resistance protein pi21 have 12.3% similarity with the nuclear transcription factor, X-box binding-like 1 (NFX) type zinc finger domain of Pi54 protein. For the first time, we reported that Pi54 (Pi-k(h)-Tetep), a rice blast resistance (R) protein have a small zinc finger domain of NFX type located on the C-terminal in between NBS and LRR domains of the R-protein. Compositional analysis depicted by the helical wheel diagram revealed the presence of a hydrophobic region within this domain which might help in exposing the LRR region for a possible R-Avr interaction. This domain is unique among all other cloned plant disease resistance genes and might play an important role in broad-spectrum nature of rice blast resistance gene Pi54.
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spelling pubmed-34197132012-08-22 Comparative Analysis of Zinc Finger Proteins Involved in Plant Disease Resistance Gupta, Santosh Kumar Rai, Amit Kumar Kanwar, Shamsher Singh Sharma, Tilak R. PLoS One Research Article A meta-analysis was performed to understand the role of zinc finger domains in proteins of resistance (R) genes cloned from different crops. We analyzed protein sequences of seventy R genes of various crops in which twenty six proteins were found to have zinc finger domains along with nucleotide binding sites - leucine rice repeats (NBS-LRR) domains. We identified thirty four zinc finger domains in the R proteins of nine crops and were grouped into 19 types of zinc fingers. The size of individual zinc finger domain within the R genes varied from 11 to 84 amino acids, whereas the size of proteins containing these domains varied from 263 to 1305 amino acids. The biophysical analysis revealed that molecular weight of Pi54 zinc finger was lowest whereas the highest one was found in rice Pib zinc finger named as Transposes Transcription Factor (TTF). The instability (R(2) = 0.95) and the aliphatic (R(2) = 0.94) indices profile of zinc finger domains follows the polynomial distribution pattern. The pairwise identity analysis showed that the Lin11, Isl-1 & Mec-3 (LIM) zinc finger domain of rice blast resistance protein pi21 have 12.3% similarity with the nuclear transcription factor, X-box binding-like 1 (NFX) type zinc finger domain of Pi54 protein. For the first time, we reported that Pi54 (Pi-k(h)-Tetep), a rice blast resistance (R) protein have a small zinc finger domain of NFX type located on the C-terminal in between NBS and LRR domains of the R-protein. Compositional analysis depicted by the helical wheel diagram revealed the presence of a hydrophobic region within this domain which might help in exposing the LRR region for a possible R-Avr interaction. This domain is unique among all other cloned plant disease resistance genes and might play an important role in broad-spectrum nature of rice blast resistance gene Pi54. Public Library of Science 2012-08-15 /pmc/articles/PMC3419713/ /pubmed/22916136 http://dx.doi.org/10.1371/journal.pone.0042578 Text en © 2012 Gupta et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Gupta, Santosh Kumar
Rai, Amit Kumar
Kanwar, Shamsher Singh
Sharma, Tilak R.
Comparative Analysis of Zinc Finger Proteins Involved in Plant Disease Resistance
title Comparative Analysis of Zinc Finger Proteins Involved in Plant Disease Resistance
title_full Comparative Analysis of Zinc Finger Proteins Involved in Plant Disease Resistance
title_fullStr Comparative Analysis of Zinc Finger Proteins Involved in Plant Disease Resistance
title_full_unstemmed Comparative Analysis of Zinc Finger Proteins Involved in Plant Disease Resistance
title_short Comparative Analysis of Zinc Finger Proteins Involved in Plant Disease Resistance
title_sort comparative analysis of zinc finger proteins involved in plant disease resistance
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3419713/
https://www.ncbi.nlm.nih.gov/pubmed/22916136
http://dx.doi.org/10.1371/journal.pone.0042578
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