In this study, we report the first co-crystal structure of SPS from Thermosynechococcus elongatus with UDP and sucrose-6-phosphate (S6P). 1. A novel α1-2-fucosyltransferase from Thermosynechococcus elongatus BP-1 (Te2FT) with high fucosyltransferase activity and low donor hydrolysis activity was discovered and characterized. The Role of Arg13 in Protein Phosphatase M tPphA from. ›Thermosynechococcus elongatus BP-1. The complete segregation of the T. elongatusNdhP-sfGFP-His mutant was confirmed by PCR analysis (Fig. These proteins plus CyanoQ isolated here were used to raise antibodies in rabbit. PCC 6803 also shows decreased electron transfer from Y Z to P 680 and only 62% of wild-type O 2 . ›Thermosynechococcus elongatus IAM M-273. Thermosynechococcus elongatus, a crucial photosynthetic model organism Yvonne Zilliges and Holger Dau Institut fur Experimentalphysik/Biophysik & Photosynthese, Freie Universit€at Berlin, Germany Correspondence Y. Zilliges, Institut f€ur Experimentalphysik/ Biophysik & Photosynthese, Freie Universit€at Berlin, Arnimallee 14, D-14195 . Synechococcus elongatus is rod-shaped with its cells typically greater than 2 µm in length. The PGDB was created computationally by the PathoLogic component of the Pathway Tools software (version 24 . 2001: not validly published: Parent taxon: Synechococcaceae Komárek and Anagnostidis 1995. For example, Thermosynechococcus elongatus contains only CBCRs, whereas Prochlorococcus strains and closely related Cyanobium and Synechococcus strains have lost all phytochromes and CBCRs [24,27]. Common name i. Synonym i. We found that T. elongatus displays natural transformation, and we established a simple and efficient protocol for transferring exogenous DNAs into the organism's genome. Journal: DNA Res 9:123-30 (2002) DOI: 10.1093/dnares/9.4.123 . Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1. The PGDB was created computationally by the PathoLogic component of the Pathway Tools software (version 24 . Function i. Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses . By mimicking cyclic electron flow with isolated . For example, Thermosynechococcus elongatus contains only CBCRs, whereas Prochlorococcus strains and closely related Cyanobium and Synechococcus strains have lost all phytochromes and CBCRs [24,27]. Thermosynechococcus elongatus. S. elongatus UTEX 2973 is a mutant hybrid from UTEX 625 and is most closely related to S. elongatus PCC 7942 with 99.8% similarity (Yu et al, 2015). -. The strain exhibits its highest growth rate around 55 °C, can withstand up to 15% CO 2, and up to 0.5 M concentration of sodium bicarbonate.The strain is also capable of resisting a 200 ppm concentration of NO and . Based on their phylogenetic prediction of this new class of enzymes, Motomura and colleagues first validated PPK2s from M. ruber, Meiothermus silvanus, Deinococcus geothermalis, Thermosynechococcus elongatus, and D. radiodurans as capable of polyP-driven ATP synthesis from AMP . Terminal (leaf) node. It typically contains 2-3 thylakoid membrane layers forming evenly spaced concentric rings and its carboxysomes and polyphosphate bodies are located in the central cytoplasmic region (Image 1). -. The proteins can be easily purified, characterized for biochemical and biophysical properties, and crystallized. Genetics The genes encoding SQS were isolated from the hopane-producing bacteria Thermosynechococcus elongatus BP-1, Bradyrhizobium japonicum, and Zymomonas mobilis and cloned into an Escherichia coli expression system. PCC 6803. 57°C, and their proteins are highly stable. Cryo- EM structure of the Thermosynechococcus elongatus photosystem I in the presence of cytochrome c6. Thermosynechococcus elongatus BP1 is a thermophilic strain of cyanobacteria that has an optimum growth at 57°C, and according to previous analysis by Yamaoka et al, T elongatus BP1 cannot survive at a temperature below 30°C. Using a heterologous expression system, it was demonstrated that this protein promotes Rubisco assembly in Escherichia coli cells. The strain exhibits its highest growth rate around 55 °C, can withstand up to 15% CO 2, and up to 0.5 M concentration of sodium bicarbonate.The strain is also capable of resisting a 200 ppm concentration of NO and . 3). However, the . Here, we show that the PC operon from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1 (cpcBACD) is functional in the mesophile Synechocystis sp. To date, however, there is no known crystal structure of SPS from plant or cyanobacteria. This review gives an overview of the current understanding of main Received 22nd March 2013, features concerning the role of copper (Cu), iron (Fe), manganese (Mn) and zinc (Zn) in plant Accepted 20th May 2013 photosynthesis as well as the mechanisms involved in their homeostasis within chloroplasts. Terminal (leaf) node. Expression of cpcBACD in an 'Olive' mutant strain of Synechocystis lacking endogenous PC resulted in high yields of thermostable PC (112 ± 1 mg g -1 DW) comparable to that . In the last decade, several strains of . A high-resolution structure of trimeric cyanobacterial Photosystem I (PSI) from Thermosynechococcus elongatus was reported as the first atomic model of PSI almost 20 years ago. -. This proteome is part of the Thermosynechococcus elongatus (strain BP-1) pan proteome ( fasta ) Busco i. The inclusion of the psbA2-encoded D1 protein of Thermosynechococcus elongatus hinders the S 2-to-S 3 transition [24], due to changes in the hydrogen-bond network around D1-P173M [25 •]. Reviewed-Annotation score: -Experimental evidence at protein level i. Thermosynechococcus elongatus strains were first grown in 1 l of DTN (Sugiura and Inoue 1999) in 3-l Erlenmeyer flasks in a rotary shaker with a CO 2-enriched atmosphere at 45°C under continuous light (80 μmol of photons m −2 s −1). The thermophilic cyanobacteria Thermosynechococcus elongatus(30) and T. vulcanus(13), which were isolated from a Japanese hot spring, grow optimally at ca. Sucrose phosphate synthase (SPS) is a well-known rate-limiting enzyme in the synthesis of sucrose. Synechococcus elongatus is a unicellular cyanobacterium that has a rapid autotrophic growth comparable to yeast. Summary of Thermosynechococcus elongatus, Strain BP-1, version 25.5 Tier 3 Uncurated Database Summary: This Pathway/Genome Database (PGDB) was generated on 15-Feb-2020 from the annotated genome of Thermosynechococcus elongatus BP-1, as obtained from RefSeq (annotation date: 06-MAR-2020). Synechococcus (from the Greek synechos, in succession, and the Greek kokkos, granule) is a unicellular cyanobacterium that is very widespread in the marine environment.Its size varies from 0.8 to 1.5 µm.The photosynthetic coccoid cells are preferentially found in well-lit surface waters where it can be very abundant (generally 1,000 to 200,000 cells per ml). We report a 3.3-angstrom-resolution cryo-electron microscopy structure of photosynthetic complex I from the cyanobacterium Thermosynechococcus elongatus. Proteins derived from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1, which performs plant-type oxygenic photosynthesis, are suitable for biochemical, biophysical, and X-ray crystallographic studies. Authors Sungwon Lee 1 , C Dale Poulter. 1978). Superfolder GFP was used for the tagging approach, as it shows enhanced thermostability compared to other GFP variants [35]. Thermosynechococcus elongatus. Summary of Thermosynechococcus elongatus, Strain BP-1, version 25.5 Tier 3 Uncurated Database Summary: This Pathway/Genome Database (PGDB) was generated on 15-Feb-2020 from the annotated genome of Thermosynechococcus elongatus BP-1, as obtained from RefSeq (annotation date: 06-MAR-2020). It was used in an efficient one-pot multienzyme (OPME) fucosylation system for the high-yield synthesis of human blood group H antigens containing β1-3-linked galactosides and an important human milk . Thermosynechococcus elongatus. It is a model system for studying the interplay of gen-etic, biochemical and physiological phenomena in pho-tosynthesis due to the availability of the complete bacterium Thermosynechococcus elongatus (Dps-Te) was chosen. "Thermosynechococcus elongatus" Katoh et al. Synonym i. In the last decade, several strains of Synechococcus elongatus have been produced in laboratory environments to include the fastest growing cyanobacteria to date, Synechococcus elongatus UTEX 2973. Thermosynechococcus elongatus BP-1 is a unicellular rod-shaped cyanobacterium, and grows at an optimal temperature 55°C (Yamaoka et al. Protein samples were separated on 18 % (w/v) polyacrylamide gels containing 6 M urea as described by Boehm et al. Other names i. Thermosynechococcus elongatus inhabits Japanese hot springs and grows optimally at around 55 C [8]. Affiliation 1 Department of . The results presented here show that the prokaryotic homolog of RAF1 from Thermosynechococcus elongatus is expressed in cyanobacterial cells and interacts with a large Rubisco subunit (RbcL). We developed an automated bioluminescence real-time monitoring system for the circadian clock in the thermophilic cyanobacterium T. elongatus BP-1 that uses a bacterial . Because of the thermostability of proteins and protein complexes and determination of the entire genome sequence ( Nakamura et al. D Density functional theory (DFT), 337 3D free energy maps chloride ion, 371, 372 dangling, 371 ILS, 368 iso-energy surfaces, 369 lipoxygenases, 369 minimal resistance paths, 370-371 molecular labyrinths, 369 Phycobilines, Sucrose Gradient, Thermosynechococcus elongatus. The Benchmarking Universal Single-Copy Ortholog (BUSCO) assessment tool is used, for eukaryotic and bacterial proteomes, to provide quantitative measures of UniProt proteome data completeness in terms of expected gene content. Thermosynechococcus elongatus is an obligate photoautotrophic organism, has an extrinsic light-harvesting structure known as the phycobilisomes A high-resolution X-ray crystal structure of the trimeric PSI from Thermosynechococcus elongatus (hereafter referred to as trimer crystal structure) was reported almost 20 years ago at 2.5 Å. The most suitable growth temperature for this cyanobacterium is 57°C, which is suitable for industrial use ( Yamaoka et al., 1978 ). The expressed proteins with a His (6) tag were found exclusively in inclusion bodies when no additives were used in the buffer. All-atom molecular dynamics (MD) simulation was used to investigate the solution structure and dynamics of the photosynthetic pigment protein complex photosystem I (PSI) from Thermosynechococcus elongatus embedded in a toroidal belt of n-dodecyl-β-d-maltoside (DDM) detergent.Evaluation of root-mean-square deviations (RMSDs) relative to the known crystal structure show that the protein complex . 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