Cloning and Analysis of BnMPK4, A Novel MAP Kinase Gene Induced by Oligochitosan in Brassica napus

2008 ◽  
Vol 34 (5) ◽  
pp. 743-747 ◽  
Author(s):  
Heng YIN
Planta ◽  
2008 ◽  
Vol 229 (3) ◽  
pp. 485-495 ◽  
Author(s):  
Xiao-juan Zong ◽  
Da-peng Li ◽  
Ling-kun Gu ◽  
De-quan Li ◽  
Li-xia Liu ◽  
...  

2018 ◽  
Vol 19 (12) ◽  
pp. 2590-2602 ◽  
Author(s):  
Xiaoguo Zhu ◽  
Jia Guo ◽  
Fuxin He ◽  
Yang Zhang ◽  
Chenglong Tan ◽  
...  

2008 ◽  
Vol 117 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Huini Xu ◽  
Xiufeng Wang ◽  
Xudong Sun ◽  
Qinghua Shi ◽  
Fengjuan Yang ◽  
...  

2006 ◽  
Vol 44 (1) ◽  
pp. 78-84 ◽  
Author(s):  
Tengguo Zhang ◽  
Yubing Liu ◽  
Lingui Xue ◽  
Shijian Xu ◽  
Tuo Chen ◽  
...  

2000 ◽  
Vol 13 (7) ◽  
pp. 724-732 ◽  
Author(s):  
Li Zheng ◽  
Mathew Campbell ◽  
Jennifer Murphy ◽  
Stephen Lam ◽  
Jin-Rong Xu

In Magnaporthe grisea, a well-conserved mitogen-activated protein (MAP) kinase gene, PMK1, is essential for fungal pathogenesis. In this study, we tested whether the same MAP kinase is essential for plant infection in the gray mold fungus Botrytis cinerea, a necrotrophic pathogen that employs infection mechanisms different from those of M. grisea. We used a polymerase chain reaction-based approach to isolate MAP kinase homologues from B. cinerea. The Botrytis MAP kinase required for pathogenesis (BMP) MAP kinase gene is highly homologous to the M. grisea PMK1. BMP1 is a single-copy gene. bmp1 gene replacement mutants produced normal conidia and mycelia but were reduced in growth rate on nutrient-rich medium. bmp1 mutants were nonpathogenic on carnation flowers and tomato leaves. Re-introduction of the wild-type BMP1 allele into the bmp1 mutant restored both normal growth rate and pathogenicity. Further studies indicated that conidia from bmp1 mutants germinated on plant surfaces but failed to penetrate and macerate plant tissues. bmp1 mutants also appeared to be defective in infecting through wounds. These results indicated that BMP1 is essential for plant infection in B. cinerea, and this MAP kinase pathway may be widely conserved in pathogenic fungi for regulating infection processes.


1995 ◽  
Vol 15 (4) ◽  
pp. 2197-2206 ◽  
Author(s):  
F Navarro-García ◽  
M Sánchez ◽  
J Pla ◽  
C Nombela

Mitogen-activated protein (MAP) kinases represent a group of serine/threonine protein kinases playing a central role in signal transduction processes in eukaryotic cells. Using a strategy based on the complementation of the thermosensitive autolytic phenotype of slt2 null mutants, we have isolated a Candida albicans homolog of Saccharomyces cerevisiae MAP kinase gene SLT2 (MPK1), which is involved in the recently outlined PKC1-controlled signalling pathway. The isolated gene, named MKC1 (MAP kinase from C. albicans), coded for a putative protein, Mkc1p, of 58,320 Da that displayed all the characteristic domains of MAP kinases and was 55% identical to S. cerevisiae Slt2p (Mpk1p). The MKC1 gene was deleted in a diploid Candida strain, and heterozygous and homozygous strains, in both Ura+ and Ura- backgrounds, were obtained to facilitate the analysis of the function of the gene. Deletion of the two alleles of the MKC1 gene gave rise to viable cells that grew at 28 and 37 degrees C but, nevertheless, displayed a variety of phenotypic traits under more stringent conditions. These included a low growth yield and a loss of viability in cultures grown at 42 degrees C, a high sensitivity to thermal shocks at 55 degrees C, an enhanced susceptibility to caffeine that was osmotically remediable, and the formation of a weak cell wall with a very low resistance to complex lytic enzyme preparations. The analysis of the functions downstream of the MKC1 gene should contribute to understanding of the connection of growth and morphogenesis in pathogenic fungi.


Life Sciences ◽  
2015 ◽  
Vol 136 ◽  
pp. 60-66 ◽  
Author(s):  
Ana Elisa Valencise Quaglio ◽  
Anthony Cesar Souza Castilho ◽  
Luiz Claudio Di Stasi

2006 ◽  
Vol 19 (4) ◽  
pp. 389-398 ◽  
Author(s):  
Rahim Mehrabi ◽  
Theo van der Lee ◽  
Cees Waalwijk ◽  
Gert H. J. Kema

Among expressed sequence tag libraries of Mycosphaerella graminicola isolate IPO323, we identified a full-length cDNA clone with high homology to the mitogen-activated protein (MAP) kinase Slt2 in Saccharomyces cerevisiae. This MAP kinase consists of a 1,242-bp open reading frame, and encodes a 414-amino-acid protein. We designated this homolog MgSlt2, generated MgSlt2 knockout strains in M. graminicola isolate IPO323, and found several altered phenotypes in vitro as well as in planta. In yeast glucose broth, MgSlt2 disruptants showed a defective polarized growth in the tip cells upon aging, causing substantial local enlargements culminating in large swollen cells containing two to four nuclei. The MgSlt2 disruptants showed a significantly increased sensitivity to several fungicides, including miconazole (2×), bifonazole (>4×), imazalil (5×), and cyproconazole (10×), and were hypersensitive to glucanase. Unlike the wild type, MgSlt2 disruptants did not produce aerial mycelia and did not melanize on potato dextrose agar. Although cytological analysis in planta showed normal penetration of wheat stomata by the germ tubes of the MgSlt2 disruptants, subsequently formed hyphal filaments frequently were unable to branch out and establish invasive growth resulting in highly reduced virulence, and prevented pycnidia formation. Therefore, we conclude that MgSlt2 is a new pathogenicity factor in M. graminicola.


Genetics ◽  
1998 ◽  
Vol 150 (1) ◽  
pp. 103-117 ◽  
Author(s):  
Mark R Lackner ◽  
Stuart K Kim

Abstract The Caenorhabditis elegans mpk-1 gene encodes a MAP kinase protein that plays an important role in Ras-mediated induction of vulval cell fates. We show that mutations that eliminate mpk-1 activity result in a highly penetrant, vulvaless phenotype. A double mutant containing a gain-of-function mpk-1 mutation and a gain-of-function mek mutation (MEK phosphorylates and activates MPK-1) exhibits a multivulva phenotype. These results suggest that mpk-1 may transduce most or all of the anchor cell signal. Epistasis analysis suggests that mpk-1 acts downstream of mek-2 (encodes a MEK homolog) and upstream of lin-1 (encodes an Ets transcription factor) in the anchor cell signaling pathway. Finally, mpk-1 may act together with let-60 ras in multiple developmental processes, as mpk-1 mutants exhibit nearly the same range of developmental phenotypes as let-60 ras mutants.


Microbiology ◽  
1998 ◽  
Vol 144 (2) ◽  
pp. 411-424 ◽  
Author(s):  
F. Navarro-Garcia ◽  
R. Alonso-Monge ◽  
H. Rico ◽  
J. Pla ◽  
R. Sentandreu ◽  
...  

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