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Extracellular proteins enhance Cupriavidus pauculus nickel tolerance and cell aggregate formation

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成果类型:
期刊论文
作者:
Wang, Mingwei;Vollstedt, Christel;Siebels, Bente;Yu, Huang;Wu, Xueling;...
通讯作者:
Zeng, WM;Streit, WR
作者机构:
[Zeng, WM; Liu, Yuandong; Yu, Runlan; Shen, Li; Wang, Mingwei; Wu, Xueling; Li, Jiaokun; Zeng, Weimin] Cent South Univ, Sch Minerals Proc & Bioengn, Changsha 410083, Peoples R China.
[Streit, Wolfgang R.; Streit, WR; Vollstedt, Christel; Wang, Mingwei] Univ Hamburg, Dept Microbiol & Biotechnol, D-22609 Hamburg, Germany.
[Siebels, Bente] Univ Hamburg, Dept Clin Chem & Lab Med, D-20246 Hamburg, Germany.
[Liu, Yuandong; Yu, Runlan; Shen, Li; Wu, Xueling; Li, Jiaokun; Zeng, Weimin] Minist Educ, Key Lab Biomet, Changsha 410083, Peoples R China.
[Yu, Huang] Univ South China, Key Discipline Lab Natl Def Biotechnol Uranium Min, Hengyang 421001, Peoples R China.
通讯机构:
[Zeng, WM ] C
[Streit, WR ] U
Cent South Univ, Sch Minerals Proc & Bioengn, Changsha 410083, Peoples R China.
Univ Hamburg, Dept Microbiol & Biotechnol, D-22609 Hamburg, Germany.
语种:
英文
关键词:
Cupriavidus;Cupriavidus pauculus;Metals, Heavy;Nickel;Proteomics;Amino acids;Biochemistry;Fluorescence spectroscopy;Heavy metals;Nickel;Polymerase chain reaction;Proteins;bacterial protein;concanavalin A;extracellular protein;fluorescein isothiocyanate;lipopolysaccharide;nickel;proteome;reactive oxygen metabolite;unclassified drug;heavy metal;nickel;Aggregate formation;Cell aggregates;Cupriavidus pauculus;Efflux pumps;Extracellular proteins;Heavy metal resistance;Model organisms;Proteinase K;Resistant bacteria;Secretome;concentration (composition);fluorescence spectroscopy;heavy metal;metabolism;polymerase chain reaction;secretion;adsorption;Article;bacterial strain;carbohydrate synthesis;cell aggregation;conceptual model;confocal laser scanning microscopy;controlled study;Cupriavidus;Cupriavidus pauculus;down regulation;fluorescence intensity;Fourier transform infrared spectroscopy;gene expression level;liquid chromatography-mass spectrometry;metal tolerance;nonhuman;open reading frame;proteomics;quantitative analysis;real time polymerase chain reaction;secretory pathway;spectrofluorometry;three dimension excitation emission matrix fluorescence spectroscopy;metabolism;Fourier transform infrared spectroscopy
期刊:
Bioresource Technology
ISSN:
0960-8524
年:
2024
卷:
393
页码:
130133
基金类别:
National Natural Science Foundation of China, NSFC, (51934009, 52074353, 52274289) National Natural Science Foundation of China, NSFC China Scholarship Council, CSC, (202006370228) China Scholarship Council, CSC National Key Research and Development Program of China, NKRDPC, (2019YFC1803604) National Key Research and Development Program of China, NKRDPC Science and Technology Program of Hunan Province, (2021NK1040) Science and Technology Program of Hunan Province
机构署名:
本校为其他机构
院系归属:
核资源工程学院
摘要:
Heavy metal-resistant bacteria secrete extracellular proteins (e-PNs). However, the role of e-PNs in heavy metal resistance remains elusive. Here Fourier Transform Infrared Spectroscopy implied that N-H, C=O and NH(2)-R played a crucial role in the adsorption and resistance of Ni(2+) in the model organism Cuprividus pauculus 1490 (C. pauculus). Proteinase K treatment reduced Ni(2+) resistance of C. pauculus underlining the essential role of e-PNs. Further three-dimension excitation-emission matrix fluorescence spectroscopy analysis demonstrated that tryptophan proteins as part of the e-PNs inc...

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