Genome-wide identification of MAPKKK genes and their response to phytoplasma stress in Chinese jujube (Ziziphus jujuba Mill.)

Abstract Backgrounds Mitogen activated protein kinase (MAPK) cascades play vital roles in signal transduction in response to various biotic and abiotic stresses. In the previous study we have identified 10 ZjMAPKs and 5 ZjMAPKKs in Chinese jujube genome and found some crucial members of ZjMAPKs and ZjMAPKKs might function importantly in the process of phytoplasma infection. But how these ZjMAPKKs were modulated by ZjMAPKKKs during this process is still elusive and little information is known about the MAPKKKs in Chinese jujube. Results In the current study, 56 ZjMAPKKKs were identified in the jujube genome and all of them contain the key S-TKc (serine/threonine protein kinase) domain which distributed in all 12 chromosomes. Phylogenetic analysis showed that these ZjMAPKKKs could be classified into two subfamilies, of which 41 belonged to Raf, and 15 to MEKK subfamily. In addition, the ZjMAPKKKs in each subfamily share the same conserved motifs and gene structures, one pair of ZjMAPKKKs (15/16) was the only tandem duplication event on Chromosome 5. Furthermore, the expression profiles of these MAPKKKs in response to phytoplasma disease were investigated by qPCR. In the three main infected tissues (witches’ broom leaves, phyllody leaves, apparent normal leaves), the ZjMAPKKK26 and 45 were significantly up regulated and the ZjMAPKKK3, 43 and 50 were down regulated. While the ZjMAPKKK4, 10, 25 and 44 were significant highly induced in the sterile cultivated tissues infected by phytoplasma, and the ZjMAPKKK7, 30, 35, 37, 40, 41, 43 and 46 were significantly down regulated. Conclusions The identification and classification analysis of ZjMAPKKKs was firstly reported and some key individual ZjMAPKKKs genes might play essential roles in response to phytoplasma infection. This could provide initial understanding for the mechanism that how the ZjMAPKKKs were involved in jujube - phytoplasma infection.

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Genome-wide identification of MAPKKK genes and their response to phytoplasma stress in Chinese jujube (Ziziphus jujuba Mill.)

10.21203/rs.2.9872/v2 ◽

2019 ◽

Author(s):

ZhiGuo Liu ◽

Lixin Wang ◽

Chaoling Xue ◽

Yuetong Chu ◽

Weilin Gao ◽

...

Keyword(s):

Protein Kinase ◽

Expression Profiles ◽

Duplication Event ◽

Kinase Domain ◽

Mitogen Activated Protein Kinase ◽

Chinese Jujube ◽

Mapk Cascades ◽

Mitogen Activated Protein ◽

Phytoplasma Infection ◽

Gene Structures

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Genome-wide identification of MAPKKK genes and their responses to phytoplasma infection in Chinese jujube (Ziziphus jujuba Mill.)

10.21203/rs.2.9872/v3 ◽

2019 ◽

Author(s):

ZhiGuo Liu(Former Corresponding Author) ◽

Lixin Wang ◽

Chaoling Xue ◽

Yuetong Chu ◽

Weilin Gao ◽

...

Keyword(s):

Protein Kinase ◽

Expression Profiles ◽

Phylogenetic Analyses ◽

Kinase Domain ◽

Mitogen Activated Protein Kinase ◽

Chinese Jujube ◽

Mapk Cascades ◽

Wide Range ◽

Phytoplasma Infection ◽

Gene Structures

Abstract Background Mitogen activated protein kinase (MAPK) cascades play vital roles in signal transduction in response to a wide range of biotic and abiotic stresses. In a previous study we identified ten ZjMAPKs and five ZjMAPKKs in the Chinese jujube genome. We found some members of ZjMAPKs and ZjMAPKKs may play key roles in the plant’s response to phytoplasma infection. But how these ZjMAPKKs are modulated by ZjMAPKKKs during the response process remains uncertain. Little information is available regarding MAPKKKs in Chinese jujube. Results A total of 56 ZjMAPKKKs were identified in the jujube genome. All contain the key S-TKc (serine/threonine protein kinase) domain which is distributed among all 12 chromosomes. Phylogenetic analyses show these ZjMAPKKKs can be classified into two subfamilies. Of these, 41 belong to the Raf subfamily and 15 to the MEKK subfamily. In addition, the ZjMAPKKKs in each subfamily share the same conserved motifs and gene structures. Only one pair of ZjMAPKKKs (15/16, on Chromosome 5) was found to be tandem duplicated. Using qPCR, the expression profiles of these MAPKKKs were investigated in response to infection with phytoplasma. In the three main infected tissues (witches’ broom leaves, phyllody leaves, apparently normal leaves), ZjMAPKKK26 and 45 were significantly up-regulated and ZjMAPKKK3, 43 and 50 were significantly down-regulated. While the ZjMAPKKK4, 10, 25 and 44 were significantly and highly induced in sterile cultivated tissues infected by phytoplasma, while ZjMAPKKK6, 7, 17, 18, 30, 34, 35, 37, 40, 41, 43, 46, 52 and 46 53 were significantly down-regulated. Conclusions For the first time, we present an identification and classification analysis of ZjMAPKKKs. Some ZjMAPKKKs genes possibly play key roles in response to phytoplasma infection. This study provides an initial understanding for the mechanisms through which ZjMAPKKKs are involved in the response of Chinese jujube to phytoplasma infection.

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Genome-wide identification of MAPKKK genes and their responses to phytoplasma infection in Chinese jujube (Ziziphus jujuba Mill.)

10.21203/rs.2.9872/v4 ◽

2020 ◽

Author(s):

ZhiGuo Liu ◽

Lixin Wang ◽

Chaoling Xue ◽

Yuetong Chu ◽

Weilin Gao ◽

...

Keyword(s):

Protein Kinase ◽

Expression Profiles ◽

Phylogenetic Analyses ◽

Kinase Domain ◽

Mitogen Activated Protein Kinase ◽

Chinese Jujube ◽

Mapk Cascades ◽

Wide Range ◽

Phytoplasma Infection ◽

Gene Structures

Abstract Background: Mitogen-activated protein kinase (MAPK) cascades play vital roles in signal transduction in response to a wide range of biotic and abiotic stresses. In a previous study, we identified ten ZjMAPKs and five ZjMAPKKs in the Chinese jujube genome. We found that some members of ZjMAPKs and ZjMAPKKs may play key roles in the plant’s response to phytoplasma infection. However, how these ZjMAPKKs are modulated by ZjMAPKKKs during the response process has not been elucidated. Little information is available regarding MAPKKKs in Chinese jujube.Results: A total of 56 ZjMAPKKKs were identified in the jujube genome. All of these kinases contain the key S-TKc (serine/threonine protein kinase) domain, which is distributed among all 12 chromosomes. Phylogenetic analyses show that these ZjMAPKKKs can be classified into two subfamilies. Specifically, 41 ZjMAPKKKs belong to the Raf subfamily, and 15 belong to the MEKK subfamily. In addition, the ZjMAPKKKs in each subfamily share the same conserved motifs and gene structures. Only one pair of ZjMAPKKKs (15/16, on chromosome 5) was found to be tandemly duplicated. Using qPCR, the expression profiles of these MAPKKKs were investigated in response to infection with phytoplasma. In the three main infected tissues (witches’ broom leaves, phyllody leaves, and apparently normal leaves), ZjMAPKKK26 and -45 were significantly upregulated, and ZjMAPKKK3, -43 and -50 were significantly downregulated. ZjMAPKKK4, -10, -25 and -44 were significantly and highly induced in sterile cultivated tissues infected by phytoplasma, while ZjMAPKKK6, -7, -17, -18, -30, -34, -35, -37, -40, -41, -43, -46, -52 and -53 were significantly downregulated.Conclusions: For the first time, we present an identification and classification analysis of ZjMAPKKKs. Some ZjMAPKKK genes may play key roles in the response to phytoplasma infection. This study provides an initial understanding of the mechanisms through which ZjMAPKKKs are involved in the response of Chinese jujube to phytoplasma infection.

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Three Main Genes in the MAPK Cascade Involved in the Chinese Jujube-Phytoplasma Interaction

Forests ◽

10.3390/f10050392 ◽

2019 ◽

Vol 10 (5) ◽

pp. 392 ◽

Cited By ~ 4

Author(s):

Zhiguo Liu ◽

Zhihui Zhao ◽

Chaoling Xue ◽

Lixin Wang ◽

Lili Wang ◽

...

Keyword(s):

Expression Profiles ◽

Plant Diseases ◽

Mitogen Activated Protein Kinase ◽

Chinese Jujube ◽

Mapk Cascades ◽

Significant Difference ◽

Mitogen Activated Protein ◽

Plant Pathogen Interaction ◽

Broom Disease ◽

Phytoplasma Infection

Chinese jujube (Ziziphus jujuba Mill.) is an important economic forest species and multipurpose fruit tree in the family of Rhamnaceae. Phytoplasmas are significant prokaryotic pathogens, associated with more than 1000 plant diseases. Jujube witches’ broom disease (JWB) is a typical phytoplasma disease, caused by ‘Candidatus Phytoplasma ziziphi’. Mitogen-activated protein kinase (MAPK) cascades are highly universal signal transduction modules and play crucial roles in regulating innate immune responses in plants. Thus, in the current study, systematical expression profiles of 10 ZjMPK and 4 ZjMPKK genes were conducted in plantlets with JWB disease, plantlets recovered from JWB disease, the tissues showing different disease symptoms, and resistant/susceptible cultivars infected by JWB phytoplasma. We found that most ZjMPK and ZjMKK genes exhibited significant up- or down-regulation expression under phytoplasma infection, but the top three differentially expressed genes (DEGs) were ZjMPK2, ZjMKK2 and ZjMKK4, which showed the biggest times of gene’s significant difference expression in all materials. Based on STRING database analysis, ZjMKK2 and ZjMPK2 were involved in the same plant-pathogen interaction pathway, and Yeast two-hybrid screening showed that ZjMKK2 could interact with ZjMPK2. Finally, we deduced a pathway of jujube MAPK cascades which response to ‘Candidatus Phytoplasma ziziphi’ infection. Our study presents the first gene-family-wide investigation on the systematical expression analysis of MAPK and MAPKK genes in Chinese jujube under phytoplasma infection. These results provide valuable information for the further research on the signaling pathway of phytoplasma infection in Chinese jujube.

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MSK1 activity is controlled by multiple phosphorylation sites

Biochemical Journal ◽

10.1042/bj20041501 ◽

2005 ◽

Vol 387 (2) ◽

pp. 507-517 ◽

Cited By ~ 119

Author(s):

Claire E. McCOY ◽

David G. CAMPBELL ◽

Maria DEAK ◽

Graham B. BLOOMBERG ◽

J. Simon C. ARTHUR

Keyword(s):

Protein Kinase ◽

P38 Mapk ◽

Kinase Domain ◽

Mitogen Activated Protein Kinase ◽

Mapk Cascades ◽

Extracellular Signal ◽

Mitogen Activated Protein ◽

Ribosomal S6 Kinase ◽

In Cells

MSK1 (mitogen- and stress-activated protein kinase) is a kinase activated in cells downstream of both the ERK1/2 (extracellular-signal-regulated kinase) and p38 MAPK (mitogen-activated protein kinase) cascades. In the present study, we show that, in addition to being phosphorylated on Thr-581 and Ser-360 by ERK1/2 or p38, MSK1 can autophosphorylate on at least six sites: Ser-212, Ser-376, Ser-381, Ser-750, Ser-752 and Ser-758. Of these sites, the N-terminal T-loop residue Ser-212 and the ‘hydrophobic motif’ Ser-376 are phosphorylated by the C-terminal kinase domain of MSK1, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain of MSK1 and therefore for the phosphorylation of MSK1 substrates in vitro. Ser-381 is also phosphorylated by the C-terminal kinase domain, and mutation of Ser-381 decreases MSK1 activity, probably through the inhibition of Ser-376 phosphorylation. Ser-750, Ser-752 and Ser-758 are phosphorylated by the N-terminal kinase domain; however, their function is not known. The activation of MSK1 in cells therefore requires the activation of the ERK1/2 or p38 MAPK cascades and does not appear to require additional signalling inputs. This is in contrast with the closely related RSK (p90 ribosomal S6 kinase) proteins, whose activity requires phosphorylation by PDK1 (3-phosphoinositide-dependent protein kinase 1) in addition to phosphorylation by ERK1/2.

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Exercise-induced mitogen-activated protein kinase signalling in skeletal muscle

Proceedings of The Nutrition Society ◽

10.1079/pns2004346 ◽

2004 ◽

Vol 63 (2) ◽

pp. 227-232 ◽

Cited By ~ 48

Author(s):

Yun Chau Long ◽

Ulrika Widegren ◽

Juleen R. Zierath

Keyword(s):

Skeletal Muscle ◽

Protein Kinase ◽

Muscle Contraction ◽

Mitogen Activated Protein Kinase ◽

Mapk Cascades ◽

Extracellular Signal ◽

Mapk Signalling ◽

Mitogen Activated Protein ◽

Exercise Induced ◽

Response To Exercise

Exercise training improves glucose homeostasis through enhanced insulin sensitivity in skeletal muscle. Muscle contraction through physical exercise is a physiological stimulus that elicits multiple biochemical and biophysical responses and therefore requires an appropriate control network. Mitogen-activated protein kinase (MAPK) signalling pathways constitute a network of phosphorylation cascades that link cellular stress to changes in transcriptional activity. MAPK cascades are divided into four major subfamilies, including extracellular signal-regulated kinases 1 and 2, p38 MAPK, c-Jun NH2-terminal kinase and extracellular signal-regulated kinase 5. The present review will present the current understanding of parallel MAPK signalling in human skeletal muscle in response to exercise and muscle contraction, with an emphasis on identifying potential signalling mechanisms responsible for changes in gene expression.

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MAPK cascade gene family in Camellia sinensis: In-silico identification, expression profiles and regulatory network analysis

BMC Genomics ◽

10.1186/s12864-020-07030-x ◽

2020 ◽

Vol 21 (1) ◽

Author(s):

Archita Chatterjee ◽

Abhirup Paul ◽

G. Meher Unnati ◽

Ruchika Rajput ◽

Trisha Biswas ◽

...

Keyword(s):

Protein Kinase ◽

Camellia Sinensis ◽

Regulatory Network ◽

Expression Profiles ◽

Abiotic Factors ◽

Mapk Cascade ◽

Mitogen Activated Protein Kinase ◽

Functional Study ◽

A Genome ◽

Mitogen Activated Protein

Abstract Background Mitogen Activated Protein Kinase (MAPK) cascade is a fundamental pathway in organisms for signal transduction. Though it is well characterized in various plants, there is no systematic study of this cascade in tea. Result In this study, 5 genes of Mitogen Activated Protein Kinase Kinase (MKK) and 16 genes of Mitogen Activated Protein Kinase (MPK) in Camellia sinensis were found through a genome-wide search taking Arabidopsis thaliana as the reference genome. Also, phylogenetic relationships along with structural analysis which includes gene structure, location as well as protein conserved motifs and domains, were systematically examined and further, predictions were validated by the results. The plant species taken for comparative study clearly displayed segmental duplication, which was a significant candidate for MAPK cascade expansion. Also, functional interaction was carried out in C. sinensis based on the orthologous genes in Arabidopsis. The expression profiles linked to various stress treatments revealed wide involvement of MAPK and MAPKK genes from Tea in response to various abiotic factors. In addition, the expression of these genes was analysed in various tissues. Conclusion This study provides the targets for further comprehensive identification, functional study, and also contributed for a better understanding of the MAPK cascade regulatory network in C. sinensis.

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Sti1 and Cdc37 Can Stabilize Hsp90 in Chaperone Complexes with a Protein Kinase

Molecular Biology of the Cell ◽

10.1091/mbc.e03-07-0480 ◽

2004 ◽

Vol 15 (4) ◽

pp. 1785-1792 ◽

Cited By ~ 56

Author(s):

Paul Lee ◽

Arsalan Shabbir ◽

Christopher Cardozo ◽

Avrom J. Caplan

Keyword(s):

Protein Kinase ◽

Kinase Domain ◽

Mitogen Activated Protein Kinase ◽

Protein Kinase Domain ◽

Relative Contribution ◽

Expression Studies ◽

Mitogen Activated Protein ◽

Gene Expression Studies ◽

Kinase Pathway

Hsp90 functions in association with several cochaperones for folding of protein kinases and transcription factors, although the relative contribution of each to the overall reaction is unknown. We assayed the role of nine different cochaperones in the activation of Ste11, a Saccharomyces cerevisiae mitogen-activated protein kinase kinase kinase. Studies on signaling via this protein kinase pathway was measured by α-factor-stimulated induction of FIG1 or lacZ, and repression of HHF1. Several cochaperone mutants tested had reduced FIG1 induction or HHF1 repression, although to differing extents. The greatest defects were in cpr7Δ, sse1Δ, and ydj1Δ mutants. Assays of Ste11 kinase activity revealed a pattern of defects in the cochaperone mutant strains that were similar to the gene expression studies. Overexpression of CDC37, a chaperone required for protein kinase folding, suppressed defects the sti1Δ mutant back to wild-type levels. CDC37 overexpression also restored stable Hsp90 binding to the Ste11 protein kinase domain in the sti1Δ mutant strain. These data suggest that Cdc37 and Sti1 have functional overlap in stabilizing Hsp90:client complexes. Finally, we show that Cns1 functions in MAP kinase signaling in association with Cpr7.

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An ste20 Homologue in Ustilago maydis Plays a Role in Mating and Pathogenicity

Eukaryotic Cell ◽

10.1128/ec.3.1.180-189.2004 ◽

2004 ◽

Vol 3 (1) ◽

pp. 180-189 ◽

Cited By ~ 32

Author(s):

David G. Smith ◽

Maria D. Garcia-Pedrajas ◽

Wei Hong ◽

Zhanyang Yu ◽

Scott E. Gold ◽

...

Keyword(s):

Protein Kinase ◽

Plant Pathogen ◽

Genomic Library ◽

Pathogenic Fungi ◽

Ustilago Maydis ◽

Kinase Domain ◽

Mapk Cascade ◽

Mitogen Activated Protein Kinase ◽

Dimorphic Fungi ◽

Mitogen Activated Protein

ABSTRACT The mitogen-activated protein kinase (MAPK) pathways are conserved from fungi to humans and have been shown to play important roles in mating and filamentous growth for both Saccharomyces cerevisiae and dimorphic fungi and in infectivity for pathogenic fungi. STE20 encodes a protein kinase of the p21-activated protein kinase family that regulates more than one of these cascades in yeasts. We hypothesized that an Ste20p homologue would play a similar role in the dimorphic plant pathogen Ustilago maydis. The full-length copy of the U. maydis gene was obtained from a genomic library; it lacked introns and was predicted to encode a protein of 826 amino acids, whose sequence confirmed its identity as the first Ste20p homologue to be isolated from a plant pathogen. The predicted protein contained both an N-terminal regulatory Cdc42-Rac interactive binding domain and a C-terminal catalytic kinase domain. Disruption of the gene smu1 resulted in a delayed mating response in a mating-type-specific manner and also in a severe reduction in disease production on maize. Unlike the Ustilago bypass of cyclase (ubc) mutations previously identified in genes in the pheromone-responsive MAPK cascade, mutation of smu1 does not by itself act as an extragenic suppressor of the filamentous phenotype of a uac1 mutant. Thus, the direct connection of Smu1p to MAPK cascade function has yet to be established. Even so, Smu1, though not absolutely required for mating, is necessary for wild-type mating and pathogenicity.

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