A Superfamily of Proteins with Novel Cysteine-Rich Repeats

Chen, Zhixiang

doi:10.1104/pp.126.2.473

Cited by 129 publications

(132 citation statements)

References 19 publications

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“…This protein has been further analyzed using bioinformatics tools. OsRMC belongs to the secreted type of DUF26 protein (Chen, 2001), with two extracellular domain-like Cys-rich motifs (DUF26). A sequence including 23 residues in the N terminus was predicted to be the signal peptide (http://www.cbs.dtu.dk/services/SignalP/; Nielsen et al, 1997;Moller et al, 2001;Supplemental Fig.…”

Section: Osrmc Is An Apoplastic Proteinmentioning

confidence: 99%

Identification of an Apoplastic Protein Involved in the Initial Phase of Salt Stress Response in Rice Root by Two-Dimensional Electrophoresis

et al. 2008

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The apoplast of plant cells, which carries out multiple functions in plant metabolism and signaling, is not only a barrier but also the linker between the environment and the protoplast. To investigate the role of apoplastic proteins in the salt stress response, 10-d-old rice (Oryza sativa) plants were treated with 200 mM NaCl for 1, 3, or 6 h, and the soluble apoplast proteins were extracted for differential analysis compared with untreated controls using two-dimensional electrophoresis. Ten protein spots that increased or decreased significantly in abundance were identified by mass spectrometry. These proteins included some well-known biotic and abiotic stress-related proteins. Among them, an apoplastic protein, with extracellular domain-like cysteine-rich motifs (DUF26), O. sativa root meander curling (OsRMC), has shown drastically increased abundance in response to salt stress during the initial phase. OsRMC RNA interference transgenic rice has been generated to assess the function of OsRMC in the salt stress response. The results show that knocking down the expression level of OsRMC in transgenic rice led to insensitive seed germination, enhanced growth inhibition, and improved salt stress tolerance to NaCl than in untransgenic plants. These results indicate that plant apoplastic proteins may have important roles in the plant salt stress response.

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Section: Osrmc Is An Apoplastic Proteinmentioning

confidence: 99%

Identification of an Apoplastic Protein Involved in the Initial Phase of Salt Stress Response in Rice Root by Two-Dimensional Electrophoresis

et al. 2008

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“…Like most RLKs, CRKs possess an extracellular domain, a single-pass transmembrane domain, and an intracellular Ser/Thr protein kinase domain (Chen, 2001). In their extracellular domain, most CRKs possess two copies of DOMAIN OF UNKNOWN FUNCTION26 (DUF26).…”

mentioning

confidence: 99%

“…The Cys residues in each DUF26 domain are predicted to form two Cys bridges, which are hypothesized to be targeted for apoplastic redox modification (Bourdais et al, 2015). In the Arabidopsis genome, there are 46 predicted CRKs, eight plasmodesmata-located proteins (PDLPs), and more than 50 Cys-rich repeat secretory proteins that possess DUF26 domains (Chen, 2001;Amari et al, 2010;Bourdais et al, 2015). PDLPs are RLPs with similarity to CRK extracellular domains (Chen, 2001).…”

mentioning

confidence: 99%

“…In the Arabidopsis genome, there are 46 predicted CRKs, eight plasmodesmata-located proteins (PDLPs), and more than 50 Cys-rich repeat secretory proteins that possess DUF26 domains (Chen, 2001;Amari et al, 2010;Bourdais et al, 2015). PDLPs are RLPs with similarity to CRK extracellular domains (Chen, 2001). PDLPs are involved in the regulation of plant cellto-cell communication, viral cell-to-cell movement, and plant immunity (Amari et al, 2010;Lee et al, 2011;Caillaud et al, 2014).…”

mentioning

confidence: 99%

“…In their extracellular domain, most CRKs possess two copies of DOMAIN OF UNKNOWN FUNCTION26 (DUF26). The DUF26 domain possesses a conserved C-X 8 -C-X 2 -C motif (Ohtake et al, 2000;Chen, 2001). The Cys residues in each DUF26 domain are predicted to form two Cys bridges, which are hypothesized to be targeted for apoplastic redox modification (Bourdais et al, 2015).…”

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confidence: 99%

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A Cysteine-Rich Protein Kinase Associates with a Membrane Immune Complex and the Cysteine Residues Are Required for Cell Death

et al. 2016

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Membrane-localized proteins perceive and respond to biotic and abiotic stresses. We performed quantitative proteomics on plasma membrane-enriched samples from Arabidopsis (Arabidopsis thaliana) treated with bacterial flagellin. We identified multiple receptor-like protein kinases changing in abundance, including cysteine (Cys)-rich receptor-like kinases (CRKs) that are up-regulated upon the perception of flagellin. CRKs possess extracellular Cys-rich domains and constitute a gene family consisting of 46 members in Arabidopsis. The single transfer DNA insertion lines CRK28 and CRK29, two CRKs induced in response to flagellin perception, did not exhibit robust alterations in immune responses. In contrast, silencing of multiple bacterial flagellin-induced CRKs resulted in enhanced susceptibility to pathogenic Pseudomonas syringae, indicating functional redundancy in this large gene family. Enhanced expression of CRK28 in Arabidopsis increased disease resistance to P. syringae. Expression of CRK28 in Nicotiana benthamiana induced cell death, which required intact extracellular Cys residues and a conserved kinase active site. CRK28-mediated cell death required the common receptor-like protein kinase coreceptor BAK1. CRK28 associated with BAK1 as well as the activated FLAGELLIN-SENSING2 (FLS2) immune receptor complex. CRK28 self-associated as well as associated with the closely related CRK29. These data support a model where Arabidopsis CRKs are synthesized upon pathogen perception, associate with the FLS2 complex, and coordinately act to enhance plant immune responses.

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The Defective in Nitrogen Fixation genes of Medicago truncatula reveal key features in the intracellular association with rhizobia

Wang

2019

The Model Legume Medicago Truncatula

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A Superfamily of Proteins with Novel Cysteine-Rich Repeats

Cited by 129 publications

References 19 publications

Identification of an Apoplastic Protein Involved in the Initial Phase of Salt Stress Response in Rice Root by Two-Dimensional Electrophoresis

Identification of an Apoplastic Protein Involved in the Initial Phase of Salt Stress Response in Rice Root by Two-Dimensional Electrophoresis

A Cysteine-Rich Protein Kinase Associates with a Membrane Immune Complex and the Cysteine Residues Are Required for Cell Death

The Defective in Nitrogen Fixation genes of Medicago truncatula reveal key features in the intracellular association with rhizobia

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