Bioinformatic comparison of human and higher plant phosphatomes

Abstract

The study presents the results of bioinformatic comparison of protein phosphatases from higher plants and human phosphatome (150 proteins). Based on sequence and profile comparison with known cat alytic domains, 204 plant homologues were selected from Physcomitrella patens and Arabidopsis thaliana. Clustering of joint group of plant and animal protein phosphatases revealed fundamental differences in plant and human phosphatomes. At the same time, significant differences in the sets of protein phosphatases in P. patens, A. thaliana, Orysa sativa, and Zea mays were shown. The percent indicators (Ident. (%) -identity, Simil. (%) -similarity, Gap. (%) -gaps) of sequence similarity are given based on the results of pairwise alignment of catalytic domain of human protein phosphatase and appropriate region of the plant homologue. The percent indicators (Ident. (%) -identity, Simil. (%) -similarity, Gap. (%) -gaps) of sequence similarity are given based on the results of pairwise alignment of catalytic domain of human protein phosphatase and appropriate region of the plant homologue.

Protein phosphatases potentially associated with regulation of microtubules, their spatial structure reconstruction and analysis

“…In addition, significant differences were found between phosphatomes of different higher plants and phylogenetic distinctions exist between phosphatomes in mosses, dicots, and monocots. United group of 175 protein plant phosphatases from Arabidopsis (113 serine/threonine‐specific, 36 tyrosine‐specific and 26 aspartate—specific protein phosphatases) (Samofalova et al, ) formed the basis for current research. For example, the sequences of Arabidopsis PP1 (P30366), PP2A (Q07099) and PP4/PPX (P48529) were used for BLASTp‐search of three new types serine/threonine‐specific protein phosphatases capable to dephosphorylate α‐, β‐ and γ‐tubulin.…”

A Journey Through Plant Cytoskeleton: Hot Spots in Signaling and Functioning

“…At same time, higher plant phosphatomes were reconstructed already (Samofalova et al, ) and among this set of plant proteins individual protein phosphatases potentially involved in regulation of MT dynamics and structure were identified (Samofalova et al, 2017). The homology of selected plant proteins and known protein phosphatase regulating structure and dynamics of MTs was confirmed on the basis of the results of their structural alignment, molecular dynamics, and conservativity in positions of functional importance.…”

A journey through a plant cytoskeleton: Hot spots in signaling and functioning

“…At the same time, higher plant phosphatomes have been reconstructed already (Samofalova et al, ) and among this set of plant proteins, individual protein phosphatases potentially involved in the regulation of MT dynamics and structure were identified (Samofalova et al, ). The homology of selected plant proteins and known protein phosphatases regulating structure and dynamics of MTs was confirmed on the basis of the results of their structural alignment, molecular dynamics and conservatism in positions of functional importance.…”