Extracellular proteins enhance Cupriavidus pauculus nickel tolerance and cell aggregate formation
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Extracellular proteins enhance Cupriavidus pauculus nickel tolerance and cell aggregate formation. / Wang, Mingwei; Vollstedt, Christel; Siebels, Bente; Yu, Huang; Wu, Xueling; Shen, Li; Li, Jiaokun; Liu, Yuandong; Yu, Runlan; Streit, Wolfgang R; Zeng, Weimin.
in: BIORESOURCE TECHNOL, Jahrgang 393, 02.2024, S. 130133.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Extracellular proteins enhance Cupriavidus pauculus nickel tolerance and cell aggregate formation
AU - Wang, Mingwei
AU - Vollstedt, Christel
AU - Siebels, Bente
AU - Yu, Huang
AU - Wu, Xueling
AU - Shen, Li
AU - Li, Jiaokun
AU - Liu, Yuandong
AU - Yu, Runlan
AU - Streit, Wolfgang R
AU - Zeng, Weimin
N1 - Copyright © 2023 Elsevier Ltd. All rights reserved.
PY - 2024/2
Y1 - 2024/2
N2 - 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 NH2-R played a crucial role in the adsorption and resistance of Ni2+ in the model organism Cuprividus pauculus 1490 (C. pauculus). Proteinase K treatment reduced Ni2+ 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 increased significantly with Ni2+ treatment. Proteomic and quantitative real-time polymerase chain reaction data indicated that major changes were induced in the metabolism of C. pauculus in response to Ni2+. Among those lipopolysaccharide biosynthesis, general secretion pathways, Ni2+-affiliated transporters and multidrug efflux play an essential role in Ni2+ resistance. Altogether the results provide a conceptual model for comprehending how e-PNs contribute to bacterial resistance and adsorption of Ni2+.
AB - 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 NH2-R played a crucial role in the adsorption and resistance of Ni2+ in the model organism Cuprividus pauculus 1490 (C. pauculus). Proteinase K treatment reduced Ni2+ 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 increased significantly with Ni2+ treatment. Proteomic and quantitative real-time polymerase chain reaction data indicated that major changes were induced in the metabolism of C. pauculus in response to Ni2+. Among those lipopolysaccharide biosynthesis, general secretion pathways, Ni2+-affiliated transporters and multidrug efflux play an essential role in Ni2+ resistance. Altogether the results provide a conceptual model for comprehending how e-PNs contribute to bacterial resistance and adsorption of Ni2+.
KW - Nickel
KW - Proteomics
KW - Metals, Heavy/metabolism
KW - Cupriavidus/metabolism
U2 - 10.1016/j.biortech.2023.130133
DO - 10.1016/j.biortech.2023.130133
M3 - SCORING: Journal article
C2 - 38043689
VL - 393
SP - 130133
JO - BIORESOURCE TECHNOL
JF - BIORESOURCE TECHNOL
SN - 0960-8524
ER -