Abstract:
:Thaumatin-like proteins (TLPs) are the products of a large, highly complex gene family involved in host defense. TLPs also belong to the pathogenesis-related family 5 (PR-5) of plant defense proteins. Most TLPs exhibit potential antifungal activities, and their accumulation in the plant is related to many physiological processes. In this study, a gene encoding TLP named permatin with an open reading frame of 678 bp encoding a protein of 225 amino acids with a calculated molecular mass of 23.5 kDa was cloned from naked oat leaves. Phylogenetic analysis revealed that permatin shares high homology with a number of other TLPs among diverse taxa. Model of structure by homology modeling showed that permatin consists of an acidic cleft region consistent with most TLPs. Recombinant NusA-permatin was overexpressed in Escherichia coli strain BL21 and purified by Heparin column combined with Sephacryl S-200 column. The protein exhibited antifungal activity to Fusarium oxysporum (half maximal inhibitory concentration, IC50 = 21.42 μM). Morphological observation showed that NusA-permatin can induce mycelium deformation of F. oxysporum, the cell membrane is blurred, and the diaphragm is not obvious. NusA-permatin also causes membrane permeabilization and reactive oxygen species accumulation in the mycelium of F. oxysporum. Permatin may play an important role in the disease resistance responses of plants against pathogen attacks through its antifungal activity.
journal_name
Probiotics Antimicrob Proteinsjournal_title
Probiotics and antimicrobial proteinsauthors
Liu J,Han D,Shi Ydoi
10.1007/s12602-018-9422-ysubject
Has Abstractpub_date
2019-03-01 00:00:00pages
299-309issue
1eissn
1867-1306issn
1867-1314pii
10.1007/s12602-018-9422-yjournal_volume
11pub_type
杂志文章abstract::It has been recently shown, that certain strains/isolates of Bacillus subtilis can be used as a probiotic for humans. The production of the macrocyclic sactibiotic subtilosin in B. subtilis ATCC 6633 is highly regulated. To improve the subtilosin productivity of B. subtilis, different growth conditions were compared f...
journal_title:Probiotics and antimicrobial proteins
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journal_title:Probiotics and antimicrobial proteins
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journal_title:Probiotics and antimicrobial proteins
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journal_title:Probiotics and antimicrobial proteins
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journal_title:Probiotics and antimicrobial proteins
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doi:10.1007/s12602-016-9222-1
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journal_title:Probiotics and antimicrobial proteins
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journal_title:Probiotics and antimicrobial proteins
pub_type: 杂志文章
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journal_title:Probiotics and antimicrobial proteins
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journal_title:Probiotics and antimicrobial proteins
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journal_title:Probiotics and antimicrobial proteins
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journal_title:Probiotics and antimicrobial proteins
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journal_title:Probiotics and antimicrobial proteins
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journal_title:Probiotics and antimicrobial proteins
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