scholarly journals Comparative Insilico Analysis of Ascorbate Peroxidase Protein Sequences from Different Plant Species

Author(s):  
Saurabh Pandey ◽  
Yogesh Kumar Negi ◽  
Soma S. Marla
F1000Research ◽  
2015 ◽  
Vol 4 ◽  
pp. 474 ◽  
Author(s):  
Leos Kral

The centromeric protein CENP-C is a base component of the kinetochore. This protein, along with CENP-A has been shown to adaptively evolve in a number of animal and plant species. In order to determine if CENP-C also evolves in fish species, I attempted to retrieve fish CENP-C sequences from GenBank. No Teleostei CENP-C sequences were found either by name or by BLASTP searches with the vertebrate CENP-C motif sequence. A number of putative Teleostei protein sequences were identified in GenBank that have homology to the C-terminal cupin domain of vertebrate CENP-C. These proteins only have partial homology to the CENP-C motif, but evidence is presented that makes it likely that these fish proteins are orthologs of CENP-C. Interestingly, it was also discovered that the CENP-C motif sequence is also mostly present in M18BP1 proteins of fish and some other vertebrates but not in mammals. This finding may have implications for CENP-C and M18BP1 assembly in centromeric regions of different vertebrate taxa.


F1000Research ◽  
2016 ◽  
Vol 4 ◽  
pp. 474 ◽  
Author(s):  
Leos Kral

The centromeric protein CENP-C is a base component of the kinetochore. This protein, along with CENP-A has been shown to adaptively evolve in a number of animal and plant species. In order to determine if CENP-C also evolves in fish species, I attempted to retrieve fish CENP-C sequences from GenBank. No Teleostei CENP-C sequences were found either by name or by BLASTP searches with the vertebrate CENP-C motif sequence. A number of putative Teleostei protein sequences were identified in GenBank that have homology to the C-terminal cupin domain of vertebrate CENP-C. These proteins only have partial homology to the CENP-C motif, but evidence is presented that makes it likely that these fish proteins are orthologs of CENP-C. Interestingly, it was also discovered that the CENP-C motif sequence is also mostly present in M18BP1 proteins of fish and some other vertebrates but not in mammals. This finding may have implications for CENP-C and M18BP1 assembly in centromeric regions of different vertebrate taxa.


2020 ◽  
Author(s):  
Qi Zheng ◽  
Kristina Majsec ◽  
Fumiaki Katagiri

ABSTRACTAmong eight Arabidopsis CaM-Binding Protein (CBP) 60 family members, AtCBP60g and AtSARD1 are partially functionally redundant, major positive immune regulators while AtCBP60a is a negative immune regulator. Phylogenetic analysis of CBP60 protein sequences of 247 diverse land plant species indicated that the immune regulator CBP60a, CBP60g, and SARD1 subfamilies diversified at divergence of Angiosperms and have been evolving very fast, suggesting strong selection pressure from pathogen effectors. We developed the Protein Evolution Analysis in Euclidean Space (PEAES) approach to investigate effects of this potential selection. We detected significant coevolutionary interactions across the immune regulator subfamilies specific to different Core Eudicot lineages, which are consistent with hypothetical coevolutionary mechanisms that protect the positive immune regulator function from being targeted by pathogen effectors. Thus, fast coevolution across the subfamilies with overlapping or opposing functions appears crucial to maintain resilience of the CBP60 immune regulator module against fast-evolving pathogen effectors.


Plants ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 52
Author(s):  
Jie Luo ◽  
Junhao Chen ◽  
Wenlei Guo ◽  
Zhengfu Yang ◽  
Kean-Jin Lim ◽  
...  

Due to its peculiar morphological characteristics, there is dispute as to whether the genus of Annamocarya sinensis, a species of Juglandaceae, is Annamocarya or Carya. Most morphologists believe it should be distinguished from the Carya genus while genomicists suggest that A. sinensis belongs to the Carya genus. To explore the taxonomic status of A. sinensis using chloroplast genes, we collected chloroplast genomes of 16 plant species and assembled chloroplast genomes of 10 unpublished Carya species. We analyzed all 26 species’ chloroplast genomes through two analytical approaches (concatenation and coalescence), using the entire and unique chloroplast coding sequence (CDS) and entire and protein sequences. Our results indicate that the analysis of the CDS and protein sequences or unique CDS and unique protein sequence of chloroplast genomes shows that A. sinensis indeed belongs to the Carya genus. In addition, our analysis shows that, compared to single chloroplast genes, the phylogeny trees constructed using numerous genes showed higher consistency. Moreover, the phylogenetic analysis calculated with the coalescence method and unique gene sequences was more robust than that done with the concatenation method, particularly for analyzing phylogenetically controversial species. Through the analysis, our results concluded that A. sinensis should be called C. sinensis.


Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
N Moodley ◽  
V Maharaj
Keyword(s):  

Planta Medica ◽  
2009 ◽  
Vol 75 (09) ◽  
Author(s):  
J Táborský ◽  
M Kunt ◽  
P Kloucek ◽  
L Kokoska

Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
V Roumy ◽  
AL Gutierrez-Choquevilca ◽  
JP Lopez Mesia ◽  
L Ruiz ◽  
J Ruiz ◽  
...  

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