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Acaryochloris marina strain:MBIC10699

ABSTRACT: Whole genome sequencing of Acaryochloris sp MBIC10699

PROVIDER: PRJDB13468 | ENA |

REPOSITORIES: ENA

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			Action	DRS
		Other
	DRR374621_1.fastq.gz	Fastqsanger.gz
	DRR374621_2.fastq.gz	Fastqsanger.gz
	DRR374622_1.fastq.gz	Fastqsanger.gz

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The complex transcriptional response of Acaryochloris marina to different oxygen levels

Project description:Ancient oxygenic photosynthetic prokaryotes produced oxygen as a waste product, but existed for a long time under an oxygen-free (anoxic) atmosphere, before an oxic atmosphere emerged. The change in oxygen levels in the atmosphere influenced the chemistry and structure of many enzymes that contained prosthetic groups that were inactivated by oxygen. In the genome of Acaryochloris marina, multiple gene copies exist for proteins that are normally encoded by a single gene copy in other cyanobacteria. Using high throughput RNA sequencing to profile transcriptome responses from cells grown under microoxic and hyperoxic conditions, we detected 8446 transcripts out of the 8462 annotated genes in the Cyanobase database. Two thirds of the 50 most abundant transcripts are key proteins in photosynthesis. Microoxic conditions negatively affected the levels of expression of genes encoding photosynthetic complexes, with the exception of some subunits. In addition to the known regulation of the multiple copies of psbA, we detected a similar transcriptional pattern for psbJ and psbU, which might play a key role in the altered components of photosystem II. Furthermore, regulation of genes encoding proteins important for reactive oxygen species-scavenging is discussed at genome level, including, for the first time, specific small RNAs having possible regulatory roles under varying oxygen levels.

2017-02-19 | GSE89387 | GEO

Acaryochloris marina

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Project description:The aim of this project is to identify, by bottom-up proteomic analysis, one or both representatives of two classes of 8-vinyl reductase in an Acaryochloris marina cell lysate. This enzyme is responsible for the conversion of the C8 vinyl group in the chlorophyll precursor Mg-divinyl-protochlorophyllide to ethyl as part of the chlorphyll biosynthesis pathway. Both putative 8VRs, NmrA and FrhB were detected.

2020-05-26 | PXD003139 | Pride

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Acaryochloris marina

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Expression analysis of motile strain of Sphingomonas sp. A1

Project description:Investigation of whole genome gene expression level in motile strain of Sphingomonas. sp A1 All flagellar genes in motile strain of Sphingomonas. sp A1 are highly transcribed.

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A biliverdin-binding cyanobacteriochrome from the chlorophyll d-bearing cyanobacterium Acaryochloris marina.

Project description:Cyanobacteriochromes (CBCRs) are linear tetrapyrrole-binding photoreceptors in cyanobacteria that absorb visible and near-ultraviolet light. CBCRs are divided into two types based on the type of chromophore they contain: phycocyanobilin (PCB) or phycoviolobilin (PVB). PCB-binding CBCRs reversibly photoconvert at relatively long wavelengths, i.e., the blue-to-red region, whereas PVB-binding CBCRs reversibly photoconvert at shorter wavelengths, i.e., the near-ultraviolet to green region. Notably, prior to this report, CBCRs containing biliverdin (BV), which absorbs at longer wavelengths than do PCB and PVB, have not been found. Herein, we report that the typical red/green CBCR AM1_1557 from the chlorophyll d-bearing cyanobacterium Acaryochloris marina can bind BV almost comparable to PCB. This BV-bound holoprotein reversibly photoconverts between a far red light-absorbing form (Pfr, ?max = 697?nm) and an orange light-absorbing form (Po, ?max = 622?nm). At room temperature, Pfr fluoresces with a maximum at 730?nm. These spectral features are red-shifted by 48~77?nm compared with those of the PCB-bound domain. Because the absorbance of chlorophyll d is red-shifted compared with that of chlorophyll a, the BV-bound AM1_1557 may be a physiologically relevant feature of A. marina and is potentially useful as an optogenetic switch and/or fluorescence imager.

| S-EPMC4302295 | biostudies-literature

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