2016
DOI: 10.1007/s00253-016-7757-4
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Vital role for the J-domain protein Mdj1 in asexual development, multiple stress tolerance, and virulence of Beauveria bassiana

Abstract: Mdj1 is a member of the Hsp40 family containing a DnaJ or J domain. Here, we have examined the functions of an Mdj1 orthologue (56.68 kDa) in Beauveria bassiana, a filamentous fungal insect pathogen widely applied in biological control of insect pests. Deletion of mdj1 in B. bassiana resulted in significant growth defects on a variety of complex and minimal media. The Δmdj1 mutant exhibited not only a drastic reduction (92 %) in aerial conidiation during optimal cultivation but also a remarkable decrease (77 %… Show more

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Cited by 25 publications
(20 citation statements)
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“…Pil1A and Pil1B (tag loci: BBA_00276 and BBA_09711 respectively), two eisosome proteins playing opposite roles in autophagic control, were required for the fungal virulence due to blocked secretion of cuticle-degrading Pr1 proteases and inhibition of dimorphic transition in absence of each or both (Zhang et al, 2017). Mdj1 (tag locus: BBA_06930), another Hsp40 family member, also made a remarked contribution to the fungal virulence as well as conidiation capacity (Wang et al, 2017b). Aside from these hyperacetylated proteins, many more Kac proteins modified in Drpd3 were involved in cell rescue, defence and virulence (Table 1) and could likely contribute to the fungal virulence through cell response to host immunity although most of them have not been characterized in B. bassiana.…”
Section: Discussionmentioning
confidence: 99%
“…Pil1A and Pil1B (tag loci: BBA_00276 and BBA_09711 respectively), two eisosome proteins playing opposite roles in autophagic control, were required for the fungal virulence due to blocked secretion of cuticle-degrading Pr1 proteases and inhibition of dimorphic transition in absence of each or both (Zhang et al, 2017). Mdj1 (tag locus: BBA_06930), another Hsp40 family member, also made a remarked contribution to the fungal virulence as well as conidiation capacity (Wang et al, 2017b). Aside from these hyperacetylated proteins, many more Kac proteins modified in Drpd3 were involved in cell rescue, defence and virulence (Table 1) and could likely contribute to the fungal virulence through cell response to host immunity although most of them have not been characterized in B. bassiana.…”
Section: Discussionmentioning
confidence: 99%
“…Both Mas5 and Mdj1, the members of Hsp40 in B . bassiana , have been shown to be indispensable for the environmental adaptation and virulence [19, 20]. …”
Section: Discussionmentioning
confidence: 99%
“…Both Mas5 and Mdj1, the members of Hsp40 in B . bassiana , play a very important role in environmental adaptation and host infection [19, 20]. The deletion of mannitol-1-phosphate dehydrogenase (MPD) reduces the content of mannitol in B .…”
Section: Introductionmentioning
confidence: 99%
“…The same strategy for the deletion of mas5 or mdj1 and associated backbone plasmids ( Wang et al, 2016 , 2017 ) were used to delete hsf1 , sfl1 , and skn7 (Gene ID: 19887609, 19887228, and 19884300, respectively) from the wild-type strain B. bassiana ARSEF2860 (designated WT herein). Briefly, the 5′ and 3′ coding/flanking fragments of each gene were amplified from the WT via PCR with paired primers (Supplementary Table S1 ) under the action of La Taq DNA polymerase (Promega, Madison, MI, United States) and inserted into p0380-bar.…”
Section: Methodsmentioning
confidence: 99%
“…The genomic database of B. bassiana ( Xiao et al, 2012 ) has Hsf1, Sfl1, and Skn7 orthologs and 28 HSPs, which fall into the small HSP, Hsp40, Hsp60, Hsp70, Hsp90, and Hsp100 families with each containing 1–15 members. However, either three HSF or most HSP genes remain functionally unexplored because only two hsp40 genes, i.e., mas5 and mdj1 , have been characterized in B. bassiana ( Wang et al, 2016 , 2017 ). It is unclear whether Hsf1, Sfl1, and Skn7 activate different families of HSP genes in an independent or cooperative manner.…”
Section: Introductionmentioning
confidence: 99%