Comprehensive<i>in silico</i>modeling of the rice plant PRR Xa21 and its interaction with RaxX21-sY and OsSERK2

Mubassir, M. H. M.; Naser, Mohammed Abu; Abdul‐Wahab, Mohd Firdaus; Jawad, Tanvir; Alvy, Raghib Ishraq; Hamdan, Salehhuddin

doi:10.1039/d0ra01396j

Cited by 5 publications

(12 citation statements)

References 106 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, the solvent-exposed residues, x, are assumed to be associated with ligand binding. e predicted 3D structure of RLK7 is similar to other similar RLKs available [40][41][42][43][44][45].…”

Section: Structural Elucidation Of Rlk7supporting

confidence: 68%

“…e extracellular LRR domain of RLK7 is distinguished by the consensus sequence LxxLxLxxNxLxx (Figure 2), which matches well with other RLK-LRR consensus sequences found in Arabidopsis [20]. With our previously developed multipletemplate modeling approach, namely, HHpred [39,40], the top five templates (4Z5W_A, 5IXO_A, 4MNA_A, 4LXR_A, and 5JFK_A) were selected and then used to predict the 3D structure of RLK7 ectodomain (Figure 3).…”

Section: Structural Elucidation Of Rlk7supporting

confidence: 55%

See 1 more Smart Citation

How Arabidopsis Receptor-Like Kinase 7 (RLK7) Manifests: Delineating Its Structure and Function

Chowdhury

Mubassir

2022

Advances in Agriculture

Self Cite

View full text Add to dashboard Cite

Like animals, plants customarily utilize cell surface-localized receptors to keep track of environmental stimuli, specifically by plasma membrane-associated receptor-like kinases (RLKs). In comparison to other organisms, plants own a variety of RLKs, which insinuates that ligand-receptor-facilitated molecular mechanisms regulate an array of processes during plant development. Here, we take up Arabidopsis receptor-like kinase 7 (RLK7), which shares the archetypal structure of transmembrane receptor kinases accompanied by a receptor-like ectodomain comprising of leucine-rich repeats (LRRs) along with a functional intracellular kinase domain. Interestingly, this distinctive receptor-like kinase not only orchestrates crucial steps during plant development, including the regulation of seed longevity, dormancy, and seed germination speed, but also plays a role in oxidative stress tolerance, salt stress tolerance, and pattern-triggered immunity. This review deciphers the sequence and structure and evaluates existing knowledge of the function and expression pattern of RLK7.

show abstract

Section: Structural Elucidation Of Rlk7supporting

confidence: 68%

Section: Structural Elucidation Of Rlk7supporting

confidence: 55%

How Arabidopsis Receptor-Like Kinase 7 (RLK7) Manifests: Delineating Its Structure and Function

Chowdhury

Mubassir

2022

Advances in Agriculture

Self Cite

View full text Add to dashboard Cite

show abstract

“…PROCHECK Ramachandran plot of the rice Xa21 protein model generated by the HHpred server showed that 99.2% of residues in the model were in the allowed region (78.9% in the most favored, 18.4% in the additionally allowed, 1.9% in generously allowed and 0.8% in disallowed regions). The model generated by PHYRE2 for the same protein had 4% less residues in the most favored regions [ 40 ]. Similar results were described for rice cytokinin oxidase/dehydrogenase 2 (CKX2) [ 41 ].…”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization and Expression of Four Aquaporin Genes in Impatiens walleriana during Drought Stress and Recovery

Đurić

Subotić

Prokić

et al. 2021

Plants

View full text Add to dashboard Cite

Aquaporins comprise a large group of transmembrane proteins responsible for water transport, which is crucial for plant survival under stress conditions. Despite the vital role of aquaporins, nothing is known about this protein family in Impatiens walleriana, a commercially important horticultural plant, which is sensitive to drought stress. In the present study, attention is given to the molecular characterization of aquaporins in I. walleriana and their expression during drought stress and recovery. We identified four I. walleriana aquaporins: IwPIP1;4, IwPIP2;2, IwPIP2;7 and IwTIP4;1. All of them had conserved NPA motifs (Asparagine-Proline-Alanine), transmembrane helices (TMh), pore characteristics, stereochemical properties and tetrameric structure of holoprotein. Drought stress and recovery treatment affected the aquaporins expression in I. walleriana leaves, which was up- or downregulated depending on stress intensity. Expression of IwPIP2;7 was the most affected of all analyzed I. walleriana aquaporins. At 15% and 5% soil moisture and recovery from 15% and 5% soil moisture, IwPIP2;7 expression significantly decreased and increased, respectively. Aquaporins IwPIP1;4 and IwTIP4;1 had lower expression in comparison to IwPIP2;7, with moderate expression changes in response to drought and recovery, while IwPIP2;2 expression was of significance only in recovered plants. Insight into the molecular structure of I. walleriana aquaporins expanded knowledge about plant aquaporins, while its expression during drought and recovery contributed to I. walleriana drought tolerance mechanisms and re-acclimation.

show abstract

“…Lys164 of OsSERK2 interacts with Asp565 of Xa21 by forming an ionic bond within 4Å (Fig. 2c) (Mubassir et al, 2020). S2).…”

Section: Changes In Interactions Of Prominent Residues Of the Proteinsmentioning

confidence: 99%

Effect of D128N mutation on OsSERK2 in Xa21 mediated immune complex: anin-silicostudy

Alvy

Mubassir

2022

Preprint

Self Cite

View full text Add to dashboard Cite

Receptor-like kinases (RLKs) are plant proteins that form signaling circuits to transduce information through the plant cell membrane to the nucleus and activate processes that direct growth, development, stress response, and disease resistance. Upon sensing various environmental stress stimuli, RLKs interact with specific targets and recruits several other proteins to initiate the defense mechanism. Among many RLK subfamilies, leucine-rich repeat RLKs (LRR-RLKs) are the largest. Xa21, a member of LRR-RLK, is a vital receptor protein in rice plants that binds with bacterial RaxX21-sY, whereas OsSERK2 is a somatic embryogenic receptor kinase (SERK) acts as a coreceptor. This study focuses on the effect of a substitution mutation of aspartate128 with asparagine128 (D128N) in OsSERK2 on the interdependent binding pattern of the mentioned Xa21, RaxX21-sY, and OsSERK2 D128N proteins. The results showed that the D128N mutation in OsSERK2 can significantly change the interaction pattern of the critical residues of the OsSERK2 and affects its receptor-ligand (Xa21-RaxX21-sY) interaction in the complex.

show abstract

Comprehensivein silicomodeling of the rice plant PRR Xa21 and its interaction with RaxX21-sY and OsSERK2

Abstract: This study exhausts bioinformatics tools to acquire the entire multi-domain rice Xa21 protein structure and analyzes its interactions with its PAMP RaxX21-sY and co-receptor OsSERK2.

Cited by 5 publications

References 106 publications

How Arabidopsis Receptor-Like Kinase 7 (RLK7) Manifests: Delineating Its Structure and Function

How Arabidopsis Receptor-Like Kinase 7 (RLK7) Manifests: Delineating Its Structure and Function

Molecular Characterization and Expression of Four Aquaporin Genes in Impatiens walleriana during Drought Stress and Recovery

Effect of D128N mutation on OsSERK2 in Xa21 mediated immune complex: anin-silicostudy

Contact Info

Product

Resources

About