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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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 |
work_keys_str_mv |
AT huichuntong prokaryoticaquaporins AT qingqinghu prokaryoticaquaporins AT linzhu prokaryoticaquaporins AT xiuzhudong prokaryoticaquaporins |
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