2019
DOI: 10.1128/jb.00740-18
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Light Modulates the Physiology of NonphototrophicActinobacteria

Abstract: Light is a source of energy and an environmental cue that is available in excess in most surface environments. In prokaryotic systems, conversion of light to energy by photoautotrophs and photoheterotrophs is well understood, but the conversion of light to information and the cellular response to that information have been characterized in only a few species. Our goal was to explore the response of freshwaterActinobacteria, which are ubiquitous in illuminated aquatic environments, to light. We found thatActino… Show more

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Cited by 31 publications
(52 citation statements)
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“…S1). Maresca et al (2019) reported that Aurantimicrobium spp. grow more rapidly in the light than in the dark.…”
Section: Resultsmentioning
confidence: 99%
“…S1). Maresca et al (2019) reported that Aurantimicrobium spp. grow more rapidly in the light than in the dark.…”
Section: Resultsmentioning
confidence: 99%
“…Lactobacillales is considered a beneficial gut bacteria, playing a role in infection control, metabolism regulation, and inflammation/allergy modulation ( Pessione, 2012 ). As mentioned above, Actinobacteria , which may be modulated by light, are able to coordinate organic carbon uptake and utilization, accompanied by the production of photosynthate that enhances growth during the daytime ( Maresca et al., 2019 ). Actinobacteria have been found to be reduced during periodontal diseases ( Kornman and Loesche, 1982 ; Kanoe et al., 1995 ) and metabolic diseases ( Long et al., 2017 ).…”
Section: Discussionmentioning
confidence: 99%
“…Photolyase-related proteins in GL MAGs were identified by searching for the following features: K01669, COG0415, PF03441, PF00875, PF04244, SSF48173, SSF52425. Reference proteins (n=56) spanning the previously defined families of photolyases and cryptochromes (33) were obtained from UniProt, along with aquatic bacterial sequences described by Maresca and colleagues (34). The reference sequences were aligned using MAFFT (27), and sequences from GL MAGs were added using the MAFFT --addfragments option.…”
Section: Extended Methodsmentioning
confidence: 99%
“…The other shares an FAD-binding domain with photolyases but the C-terminal region has no recognizable domains (Fig 5b). This protein is widespread in aquatic bacteria and has not been functionally characterized, though an actinobacterial homolog was suggested to be involved in light sensing and regulation (86). Beyond photolyases, NspiraGL also encode uracil-DNA glycosylase (UNG), which removes misincorporated uracil from DNA.…”
Section: Great Lakes Nitrospira Reveal Adaptations To Sunlit Oxic Envmentioning
confidence: 99%