|Appears in Collections:||Biological and Environmental Sciences Journal Articles|
|Peer Review Status:||Refereed|
|Title:||Bacterial survival under extreme UV radiation: A comparative proteomics study of Rhodobacter sp., isolated from high altitude wetlands in Chile|
|Authors:||Perez, Vilma A|
Hengst, Martha B
Jeffrey, Wade H
|Citation:||Perez VA, Hengst MB, Kurte L, Dorador C, Jeffrey WH, Wattiez R, Molina V & Matallana-Surget S (2017) Bacterial survival under extreme UV radiation: A comparative proteomics study of Rhodobacter sp., isolated from high altitude wetlands in Chile, Frontiers in Microbiology, 8, Art. No.: 1173.|
|Abstract:||Salar de Huasco, defined as a polyextreme environment, is a high altitude saline wetland in the Chilean Altiplano (3800 m.a.s.l.), permanently exposed to the highest solar radiation doses registered in the world. We present here the first comparative proteomics study of a photoheterotrophic bacterium, Rhodobacter sp., isolated from this remote and hostile habitat. We developed an innovative experimental approach using different sources of radiation (in situ sunlight and UVB lamps), cut-off filters (Mylar, Lee filters) and a high-throughput, label-free quantitative proteomics method to comprehensively analyze the effect of seven spectral bands on protein regulation. A hierarchical cluster analysis (HCA) of 40 common proteins revealed that all conditions containing the most damaging UVB radiation induced similar pattern of protein regulation compared with UVA and visible light spectral bands. Moreover, it appeared that the cellular adaptation of Rhodobacter sp. to osmotic stress encountered in the hypersaline environment from which it was originally isolated, might further a higher resistance to damaging UV radiation. Indeed, proteins involved in the synthesis and transport of key osmoprotectants, such as glycine betaine and inositol, were found in very high abundance under UV radiation compared to the dark control, suggesting the function of osmolytes as efficient reactive oxygen scavengers. Our study also revealed a RecA-independent response and a tightly regulated network of protein quality control involving proteases and chaperones to selectively degrade misfolded and/or damaged proteins.|
|Rights:||© 2017 Pérez, Hengst, Kurte, Dorador, Jeffrey, Wattiez, Molina and Matallana-Surget. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.|
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