scholarly journals A Novel Aldo-Keto Reductase (AKR17A1) of Anabaena sp. PCC 7120 Degrades the Rice Field Herbicide Butachlor and Confers Tolerance to Abiotic Stresses in E. coli

PLoS ONE ◽  
2015 ◽  
Vol 10 (9) ◽  
pp. e0137744 ◽  
Author(s):  
Chhavi Agrawal ◽  
Sonia Sen ◽  
Shivam Yadav ◽  
Shweta Rai ◽  
Lal Chand Rai
Keyword(s):  
Abiotic Stresses ◽  
Rice Field ◽  
E Coli ◽  
Anabaena Sp ◽  
Pcc 7120

scholarly journals Isoaspartyl dipeptidase activity of plant-type asparaginases

2002 ◽  
Vol 364 (1) ◽  
pp. 129-136 ◽  
Author(s):  
Mahdi HEJAZI ◽  
Kirill PIOTUKH ◽  
Jens MATTOW ◽  
Rainer DEUTZMANN ◽  
Rudolf VOLKMER-ENGERT ◽  
...  
Keyword(s):  
Single Gene ◽  
Culture Collection ◽  
Plant Type ◽  
Protein Subunits ◽  
E Coli ◽  
Recombinant Plant ◽  
Pasteur Culture Collection ◽  
Anabaena Sp ◽  
Altered Proteins ◽  
Pcc 7120

Recombinant plant-type asparaginases from the cyanobacteria Synechocystis sp. PCC (Pasteur culture collection) 6803 and Anabaena sp. PCC 7120, from Escherichia coli and from the plant Arabidopsis thaliana were expressed in E. coli with either an N-terminal or a C-terminal His tag, and purified. Although each of the four enzymes is encoded by a single gene, their mature forms consist of two protein subunits that are generated by autoproteolytic cleavage of the primary translation products at the Gly—Thr bond within the sequence GTI/VG. The enzymes not only deamidated asparagine but also hydrolysed a range of isoaspartyl dipeptides. As various isoaspartyl peptides are known to arise from proteolytic degradation of post-translationally altered proteins containing isoaspartyl residues, and from depolymerization of the cyanobacterial reserve polymer multi-l-arginyl-poly-l-aspartic acid (cyanophycin), plant-type asparaginases may not only function in asparagine catabolism but also in the final steps of protein and cyanophycin degradation. The properties of these enzymes are compared with those of the sequence-related glycosylasparaginases.

scholarly journals Site-Specific Recombination in the Cyanobacterium Anabaena sp. Strain PCC 7120 Catalyzed by the Integrase of Coliphage HK022

2009 ◽  
Vol 191 (13) ◽  
pp. 4458-4464 ◽  
Author(s):  
Olga Melnikov ◽  
Arieh Zaritsky ◽  
Aliza Zarka ◽  
Sammy Boussiba ◽  
Natalia Malchin ◽  
...  
Keyword(s):  
Integration Host Factor ◽  
Specific Gene ◽  
Recombination Reaction ◽  
Site Specific ◽  
Site Specific Recombination ◽  
E Coli ◽  
Site Specific Integration ◽  
Cyanobacterium Anabaena ◽  
Anabaena Sp ◽  
Pcc 7120

ABSTRACT The integrase (Int) of the λ-like coliphage HK022 catalyzes the site-specific integration and excision of the phage DNA into and from the chromosome of its host, Escherichia coli. Int recognizes two different pairs of recombining sites attP × attB and attL × attR for integration and excision, respectively. This system was adapted to the cyanobacterium Anabaena sp. strain PCC 7120 as a potential tool for site-specific gene manipulations in the cyanobacterium. Two plasmids were consecutively cointroduced by conjugation into Anabaena cells, one plasmid that expresses HK022 Int recombinase and the other plasmid that carries the excision substrate PglnA -attL-T1/T2-attR-lacZ, where T1/T2 are the strong transcription terminators of rrnB, to prevent expression of the lacZ reporter under the constitutive promoter PglnA . The Int-catalyzed site-specific recombination reaction was monitored by the expression of lacZ emanating as a result of T1/T2 excision. Int catalyzed the site-specific excision reaction in Anabaena cells when its substrate was located either on the plasmid or on the chromosome with no need to supply an accessory protein, such as integration host factor and excisionase (Xis), which are indispensable for this reaction in its host, E. coli.

Functional properties of LptA and LptD in Anabaena sp. PCC 7120

2015 ◽  
Vol 396 (9-10) ◽  
pp. 1151-1162 ◽  
Author(s):  
Yi-Ching Hsueh ◽  
Eva-M. Brouwer ◽  
Julian Marzi ◽  
Oliver Mirus ◽  
Enrico Schleiff
Keyword(s):  
Outer Membrane ◽  
Lipid A ◽  
Cytoplasmic Membrane ◽  
Model Systems ◽  
Wall Function ◽  
E Coli ◽  
The Core ◽  
Anabaena Sp ◽  
Pcc 7120 ◽  
Pore Domain

Abstract Lipopolysaccharides (LPS) are central components of the outer membrane and consist of Lipid A, the core polysaccharide, and the O-antigen. The synthesis of LPS is initiated at the cytosolic face of the cytoplasmic membrane. The subsequent transport to and across the outer membrane involves multiple lipopolysaccharide transport (Lpt) proteins. Among those proteins, the periplasmic-localized LptA and the outer membrane-embedded LptD participate in the last steps of transfer and insertion of LPS into the outer membrane. While the process is described for proteobacterial model systems, not much is known about the machinery in cyanobacteria. We demonstrate that anaLptD (alr1278) of Anabaena sp. PCC 7120 is important for cell wall function and its pore domain shows a Lipid A sensitive cation-selective gating behavior. The N-terminal domain of anaLptD recognizes anaLptA (alr4067), but not ecLptA. Furthermore, anaLptA specifically interacts with the Lipid A from Anabaena sp. PCC 7120 only, while anaLptD binds to Lipid A isolated from Escherichia coli as well. Based on the comparative analysis of proteins from E. coli and Anabaena sp. we discuss the properties of the cyanobacterial Lpt system.

Expanding the Natural Products Heterologous Expression Repertoire in the Model Cyanobacterium Anabaena sp. Strain PCC 7120: Production of Pendolmycin and Teleocidin B-4

2019 ◽  
Author(s):  
Patrick Videau ◽  
Kaitlyn Wells ◽  
Arun Singh ◽  
Jessie Eiting ◽  
Philip Proteau ◽  
...  
Keyword(s):  
Natural Products ◽  
Genome Mining ◽  
Gene Clusters ◽  
Combinatorial Biosynthesis ◽  
Test Case ◽  
Biosynthetic Gene ◽  
Biosynthetic Gene Clusters ◽  
Cyanobacterium Anabaena ◽  
Anabaena Sp ◽  
Pcc 7120

Cyanobacteria are prolific producers of natural products and genome mining has shown that many orphan biosynthetic gene clusters can be found in sequenced cyanobacterial genomes. New tools and methodologies are required to investigate these biosynthetic gene clusters and here we present the use of <i>Anabaena </i>sp. strain PCC 7120 as a host for combinatorial biosynthesis of natural products using the indolactam natural products (lyngbyatoxin A, pendolmycin, and teleocidin B-4) as a test case. We were able to successfully produce all three compounds using codon optimized genes from Actinobacteria. We also introduce a new plasmid backbone based on the native <i>Anabaena</i>7120 plasmid pCC7120ζ and show that production of teleocidin B-4 can be accomplished using a two-plasmid system, which can be introduced by co-conjugation.

Target Gene Inactivation in Cyanobacterium Anabaena sp. PCC 7120

BIO-PROTOCOL ◽  
2016 ◽  
Vol 6 (15) ◽  
Author(s):  
Kangming Chen ◽  
Huilan Zhu ◽  
Liping Gu ◽  
Shengni Tian ◽  
Ruanbao Zhou
Keyword(s):  
Target Gene ◽  
Gene Inactivation ◽  
Cyanobacterium Anabaena ◽  
Anabaena Sp ◽  
Pcc 7120

scholarly journals 2‐oxoglutarate modulates the affinity of FurA for the ntcA promoter in Anabaena sp. PCC 7120

FEBS Letters ◽  
2019 ◽  
Vol 594 (2) ◽  
pp. 278-289
Author(s):  
Jorge Guío ◽  
Cristina Sarasa‐Buisan ◽  
Adrián Velázquez‐Campoy ◽  
María Teresa Bes ◽  
María F. Fillat ◽  
...  
Keyword(s):  
Anabaena Sp ◽  
Pcc 7120
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