Prokaryotic Aquaporins

Aquaporins are integral membrane proteins that facilitate the diffusion of water and other small, uncharged solutes across the cellular membrane and are widely distributed in organisms from humans to bacteria. However, the characteristics of prokaryotic aquaporins remain largely unknown. We investig...

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Main Authors: Huichun Tong, Qingqing Hu, Lin Zhu, Xiuzhu Dong
Format: Article
Language:English
Published: MDPI AG 2019-10-01
Series:Cells
Subjects:
Online Access:https://www.mdpi.com/2073-4409/8/11/1316
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spelling doaj-68e05a9a8c9949668a3c21c65268ab062020-11-25T01:23:42ZengMDPI AGCells2073-44092019-10-01811131610.3390/cells8111316cells8111316Prokaryotic AquaporinsHuichun Tong0Qingqing Hu1Lin Zhu2Xiuzhu Dong3State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, No.1 Beichen West Road, Chaoyang District, Beijing 100101, ChinaState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, No.1 Beichen West Road, Chaoyang District, Beijing 100101, ChinaState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, No.1 Beichen West Road, Chaoyang District, Beijing 100101, ChinaState Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, No.1 Beichen West Road, Chaoyang District, Beijing 100101, ChinaAquaporins are integral membrane proteins that facilitate the diffusion of water and other small, uncharged solutes across the cellular membrane and are widely distributed in organisms from humans to bacteria. However, the characteristics of prokaryotic aquaporins remain largely unknown. We investigated the distribution and sequence characterization of aquaporins in prokaryotic organisms and summarized the transport characteristics, physiological functions, and regulatory mechanisms of prokaryotic aquaporins. Aquaporin homologues were identified in 3315 prokaryotic genomes retrieved from the Kyoto Encyclopedia of Genes and Genomes (KEGG) database, but the protein clustering pattern is not completely congruent with the phylogeny of the species that carry them. Moreover, prokaryotic aquaporins display diversified aromatic/arginine constriction region (ar/R) amino acid compositions, implying multiple functions. The typical water and glycerol transport characterization, physiological functions, and regulations have been extensively studied in <i>Escherichia coli</i> AqpZ and GlpF. A <i>Streptococcus</i> aquaporin has recently been verified to facilitate the efflux of endogenous H<sub>2</sub>O<sub>2</sub>, which not only contributes to detoxification but also to species competitiveness, improving our understanding of prokaryotic aquaporins. Furthermore, recent studies revealed novel regulatory mechanisms of prokaryotic aquaporins at post-translational level. Thus, we propose that intensive investigation on prokaryotic aquaporins would extend the functional categories and working mechanisms of these ubiquitous, intrinsic membrane proteins.https://www.mdpi.com/2073-4409/8/11/1316aquaporinsfacilitated diffusionprokaryoteselective filtertetramerhydrogen peroxide
collection DOAJ
language English
format Article
sources DOAJ
author Huichun Tong
Qingqing Hu
Lin Zhu
Xiuzhu Dong
spellingShingle Huichun Tong
Qingqing Hu
Lin Zhu
Xiuzhu Dong
Prokaryotic Aquaporins
Cells
aquaporins
facilitated diffusion
prokaryote
selective filter
tetramer
hydrogen peroxide
author_facet Huichun Tong
Qingqing Hu
Lin Zhu
Xiuzhu Dong
author_sort Huichun Tong
title Prokaryotic Aquaporins
title_short Prokaryotic Aquaporins
title_full Prokaryotic Aquaporins
title_fullStr Prokaryotic Aquaporins
title_full_unstemmed Prokaryotic Aquaporins
title_sort prokaryotic aquaporins
publisher MDPI AG
series Cells
issn 2073-4409
publishDate 2019-10-01
description Aquaporins are integral membrane proteins that facilitate the diffusion of water and other small, uncharged solutes across the cellular membrane and are widely distributed in organisms from humans to bacteria. However, the characteristics of prokaryotic aquaporins remain largely unknown. We investigated the distribution and sequence characterization of aquaporins in prokaryotic organisms and summarized the transport characteristics, physiological functions, and regulatory mechanisms of prokaryotic aquaporins. Aquaporin homologues were identified in 3315 prokaryotic genomes retrieved from the Kyoto Encyclopedia of Genes and Genomes (KEGG) database, but the protein clustering pattern is not completely congruent with the phylogeny of the species that carry them. Moreover, prokaryotic aquaporins display diversified aromatic/arginine constriction region (ar/R) amino acid compositions, implying multiple functions. The typical water and glycerol transport characterization, physiological functions, and regulations have been extensively studied in <i>Escherichia coli</i> AqpZ and GlpF. A <i>Streptococcus</i> aquaporin has recently been verified to facilitate the efflux of endogenous H<sub>2</sub>O<sub>2</sub>, which not only contributes to detoxification but also to species competitiveness, improving our understanding of prokaryotic aquaporins. Furthermore, recent studies revealed novel regulatory mechanisms of prokaryotic aquaporins at post-translational level. Thus, we propose that intensive investigation on prokaryotic aquaporins would extend the functional categories and working mechanisms of these ubiquitous, intrinsic membrane proteins.
topic aquaporins
facilitated diffusion
prokaryote
selective filter
tetramer
hydrogen peroxide
url https://www.mdpi.com/2073-4409/8/11/1316
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AT qingqinghu prokaryoticaquaporins
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