Microevolution in Cyanobacteria: Re-sequencing a Motile Substrain of Synechocystis sp. PCC 6803

Trautmann, Danika; Voß, Björn; Wilde, Annegret; Al‐Babili, Salim; Hess, Wolfgang R.

doi:10.1093/dnares/dss024

Cited by 142 publications

(167 citation statements)

References 50 publications

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“…Our very recent in vitro analysis clearly demonstrated that the KaiC1 protein of Synechocystis exhibits autophosphorylation activity and that KaiC1's kinase activity is positively affected by KaiA (53). On the other hand, laboratory substrains of Synechocystis have evolved over the course of the last 2 decades, with different phenotypes and single nucleotide polymorphisms (SNPs), but mutations in known circadian clock-related genes were not found in the Synechocystis substrain "PCC-M" used here (54). However, one has to consider that the number of previously reported circadian clockregulated genes is very small for Synechocystis.…”

Section: Discussionmentioning

confidence: 75%

Daily Expression Pattern of Protein-Encoding Genes and Small Noncoding RNAs in Synechocystis sp. Strain PCC 6803

Beck

Hertel

Rediger

et al. 2014

Appl Environ Microbiol

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Section: Discussionmentioning

confidence: 75%

Daily Expression Pattern of Protein-Encoding Genes and Small Noncoding RNAs in Synechocystis sp. Strain PCC 6803

Beck

Hertel

Rediger

et al. 2014

Appl Environ Microbiol

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“…PCC-N and Synechocystis sp. PCC-P) by Narikawa et al (2011) that contain known genetic differences from Synechocystis (Trautmann et al, 2012). Additionally, the variations in response could be caused by differences in the location of the disruption.…”

Section: Discussionmentioning

confidence: 99%

“…SynEtr1 is one of several phytochrome-like proteins identified in Synechocystis; some of these proteins, including SynEtr1, are involved in the regulation of phototaxis (Kaneko et al, 1996;Hughes et al, 1997;Yeh et al, 1997;Park et al, 2000;Wilde et al, 2002;Narikawa et al, 2011;Song et al, 2011 (Ikeuchi and Tabata, 2001;Trautmann et al, 2012), failed to move in response to directional white light in the absence or presence of ethylene, indicating that ethylene affects taxis rather than growth (data not shown). The effect of ethylene on light sensitivity also was examined by performing phototaxis assays in air and 1 mL L 21 ethylene at fluence rates ranging from 3.5 to 30 mmol m 22 s 21 white light.…”

Section: Application Of Ethylene Affects Phototaxis Via Synetr1mentioning

confidence: 99%

Ethylene Regulates the Physiology of the Cyanobacterium Synechocystis sp. PCC 6803 via an Ethylene Receptor

2016

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Ethylene is a plant hormone that plays a crucial role in the growth and development of plants. The ethylene receptors in plants are well studied, and it is generally assumed that they are found only in plants. In a search of sequenced genomes, we found that many bacterial species contain putative ethylene receptors. Plants acquired many proteins from cyanobacteria as a result of the endosymbiotic event that led to chloroplasts. We provide data that the cyanobacterium Synechocystis (Synechocystis sp. PCC 6803) has a functional receptor for ethylene, Synechocystis Ethylene Response1 (SynEtr1). We first show that SynEtr1 directly binds ethylene. Second, we demonstrate that application of ethylene to Synechocystis cells or disruption of the SynEtr1 gene affects several processes, including phototaxis, type IV pilus biosynthesis, photosystem II levels, biofilm formation, and spontaneous cell sedimentation. Our data suggest a model where SynEtr1 inhibits downstream signaling and ethylene inhibits SynEtr1. This is similar to the inverse-agonist model of ethylene receptor signaling proposed for plants and suggests a conservation of structure and function that possibly originated over 1 billion years ago. Prior research showed that SynEtr1 also contains a light-responsive phytochrome-like domain. Thus, SynEtr1 is a bifunctional receptor that mediates responses to both light and ethylene. To our knowledge, this is the first demonstration of a functional ethylene receptor in a nonplant species and suggests that that the perception of ethylene is more widespread than previously thought.

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“…Indeed, several laboratory strains of Synechocystis sp. PCC 6803 carry one of two forms of a truncated sll1951 open reading frame (48,49), indicating that under laboratory conditions cells with a shorter Sll1951 may have a slight growth advantage.…”

Section: Discussionmentioning

confidence: 99%

The sll1951 Gene Encodes the Surface Layer Protein of Synechocystis sp. Strain PCC 6803

Trautner

Vermaas

2013

Journal of Bacteriology

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Sll1951 is the surface layer (S-layer) protein of the cyanobacterium Synechocystis sp. strain PCC 6803. This large, hemolysin-like protein was found in the supernatant of a strain that was deficient in S-layer attachment. An sll1951 deletion mutation was introduced into Synechocystis and was easily segregated to homozygosity under laboratory conditions. By thin-section and negativestain transmission electron microscopy, a ϳ30-nm-wide S-layer lattice covering the cell surface was readily visible in wild-type cells but was absent in the ⌬sll1951 strain. Instead, the ⌬sll1951 strain displayed a smooth lipopolysaccharide surface as its most peripheral layer. In the presence of chaotropic agents, the wild type released a large (>150-kDa) protein into the medium that was identified as Sll1951 by mass spectrometry of trypsin fragments; this protein was missing in the ⌬sll1951 strain. In addition, Sll1951 was prominent in crude extracts of the wild type, indicating that it is an abundant protein. The carotenoid composition of the cell wall fraction of the ⌬sll1951 strain was similar to that of the wild type, suggesting that the S-layer does not contribute to carotenoid binding. Although the photoautotrophic growth rate of the ⌬sll1951 strain was similar to that of the wild-type strain, the viability of the ⌬sll1951 strain was reduced upon exposure to lysozyme treatment and hypo-osmotic stress, indicating a contribution of the S-layer to the integrity of the Synechocystis cell wall. This work identifies the S-layer protein in Synechocystis and shows that, at least under laboratory conditions, this very abundant, large protein has a supportive but not a critical role in the function of the cyanobacterium.

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Microevolution in Cyanobacteria: Re-sequencing a Motile Substrain of Synechocystis sp. PCC 6803

Cited by 142 publications

References 50 publications

Daily Expression Pattern of Protein-Encoding Genes and Small Noncoding RNAs in Synechocystis sp. Strain PCC 6803

Daily Expression Pattern of Protein-Encoding Genes and Small Noncoding RNAs in Synechocystis sp. Strain PCC 6803

Ethylene Regulates the Physiology of the Cyanobacterium Synechocystis sp. PCC 6803 via an Ethylene Receptor

The sll1951 Gene Encodes the Surface Layer Protein of Synechocystis sp. Strain PCC 6803

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