Functional Characterization of the Putative POT from Clostridium perfringens

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Functional Characterization of the Putative POT from Clostridium perfringens. / Gharabli, Hani; Rafiq, Maria; Iqbal, Anna; Yan, Ruyu; Aduri, Nanda G.; Sharma, Neha; Prabhala, Bala Krishna; Mirza, Osman.

In: Biology, Vol. 12, No. 5, 651, 2023.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Gharabli, H, Rafiq, M, Iqbal, A, Yan, R, Aduri, NG, Sharma, N, Prabhala, BK & Mirza, O 2023, 'Functional Characterization of the Putative POT from Clostridium perfringens', Biology, vol. 12, no. 5, 651. https://doi.org/10.3390/biology12050651

APA

Gharabli, H., Rafiq, M., Iqbal, A., Yan, R., Aduri, N. G., Sharma, N., Prabhala, B. K., & Mirza, O. (2023). Functional Characterization of the Putative POT from Clostridium perfringens. Biology, 12(5), [651]. https://doi.org/10.3390/biology12050651

Vancouver

Gharabli H, Rafiq M, Iqbal A, Yan R, Aduri NG, Sharma N et al. Functional Characterization of the Putative POT from Clostridium perfringens. Biology. 2023;12(5). 651. https://doi.org/10.3390/biology12050651

Author

Gharabli, Hani ; Rafiq, Maria ; Iqbal, Anna ; Yan, Ruyu ; Aduri, Nanda G. ; Sharma, Neha ; Prabhala, Bala Krishna ; Mirza, Osman. / Functional Characterization of the Putative POT from Clostridium perfringens. In: Biology. 2023 ; Vol. 12, No. 5.

Bibtex

@article{382dc334371945d099acbbfe4392d997,
title = "Functional Characterization of the Putative POT from Clostridium perfringens",
abstract = "Proton-coupled oligopeptide transporters (POTs) are a fundamental part of the cellular transport machinery that provides plants, bacteria, and mammals with nutrition in the form of short peptides. However, POTs are not restricted to peptide transport; mammalian POTs have especially been in focus due to their ability to transport several peptidomimetics in the small intestine. Herein, we studied a POT from Clostridium perfringens (CPEPOT), which unexpectedly exhibited atypical characteristics. First, very little uptake of a fluorescently labelled peptide β-Ala-Lys-AMCA, an otherwise good substrate of several other bacterial POTs, was observed. Secondly, in the presence of a competitor peptide, enhanced uptake of β-Ala-Lys-AMCA was observed due to trans-stimulation. This effect was also observed even in the absence of a proton electrochemical gradient, suggesting that β-Ala-Lys-AMCA uptake mediated by CPEPOT is likely through the substrate-concentration-driving exchange mechanism, unlike any other functionally characterized bacterial POTs.",
author = "Hani Gharabli and Maria Rafiq and Anna Iqbal and Ruyu Yan and Aduri, {Nanda G.} and Neha Sharma and Prabhala, {Bala Krishna} and Osman Mirza",
note = "This article belongs to the Section Biochemistry and Molecular Biology.",
year = "2023",
doi = "10.3390/biology12050651",
language = "English",
volume = "12",
journal = "Biology",
issn = "2079-7737",
publisher = "MDPI AG",
number = "5",

}

RIS

TY - JOUR

T1 - Functional Characterization of the Putative POT from Clostridium perfringens

AU - Gharabli, Hani

AU - Rafiq, Maria

AU - Iqbal, Anna

AU - Yan, Ruyu

AU - Aduri, Nanda G.

AU - Sharma, Neha

AU - Prabhala, Bala Krishna

AU - Mirza, Osman

N1 - This article belongs to the Section Biochemistry and Molecular Biology.

PY - 2023

Y1 - 2023

N2 - Proton-coupled oligopeptide transporters (POTs) are a fundamental part of the cellular transport machinery that provides plants, bacteria, and mammals with nutrition in the form of short peptides. However, POTs are not restricted to peptide transport; mammalian POTs have especially been in focus due to their ability to transport several peptidomimetics in the small intestine. Herein, we studied a POT from Clostridium perfringens (CPEPOT), which unexpectedly exhibited atypical characteristics. First, very little uptake of a fluorescently labelled peptide β-Ala-Lys-AMCA, an otherwise good substrate of several other bacterial POTs, was observed. Secondly, in the presence of a competitor peptide, enhanced uptake of β-Ala-Lys-AMCA was observed due to trans-stimulation. This effect was also observed even in the absence of a proton electrochemical gradient, suggesting that β-Ala-Lys-AMCA uptake mediated by CPEPOT is likely through the substrate-concentration-driving exchange mechanism, unlike any other functionally characterized bacterial POTs.

AB - Proton-coupled oligopeptide transporters (POTs) are a fundamental part of the cellular transport machinery that provides plants, bacteria, and mammals with nutrition in the form of short peptides. However, POTs are not restricted to peptide transport; mammalian POTs have especially been in focus due to their ability to transport several peptidomimetics in the small intestine. Herein, we studied a POT from Clostridium perfringens (CPEPOT), which unexpectedly exhibited atypical characteristics. First, very little uptake of a fluorescently labelled peptide β-Ala-Lys-AMCA, an otherwise good substrate of several other bacterial POTs, was observed. Secondly, in the presence of a competitor peptide, enhanced uptake of β-Ala-Lys-AMCA was observed due to trans-stimulation. This effect was also observed even in the absence of a proton electrochemical gradient, suggesting that β-Ala-Lys-AMCA uptake mediated by CPEPOT is likely through the substrate-concentration-driving exchange mechanism, unlike any other functionally characterized bacterial POTs.

U2 - 10.3390/biology12050651

DO - 10.3390/biology12050651

M3 - Journal article

C2 - 37237465

VL - 12

JO - Biology

JF - Biology

SN - 2079-7737

IS - 5

M1 - 651

ER -

ID: 346851172