Expression and Purification of the Transcription Factor NtcA from the Cyanobacterium Anabaena PCC 7120

1999 ◽  
Vol 17 (3) ◽  
pp. 351-357 ◽  
Author(s):  
Susanne Wisén ◽  
Fanyi Jiang ◽  
Birgitta Bergman ◽  
Bengt Mannervik
Keyword(s):  
Transcription Factor ◽  
Expression And Purification ◽  
Anabaena Pcc 7120 ◽  
Cyanobacterium Anabaena ◽  
Pcc 7120

Sodium regulation of GAF domain function

2007 ◽  
Vol 35 (5) ◽  
pp. 1032-1034 ◽  
Author(s):  
M.J. Cann
Keyword(s):  
Cyclic Nucleotides ◽  
Protein Domain ◽  
Genetic Ablation ◽  
Anabaena Pcc 7120 ◽  
Cyanobacterium Anabaena ◽  
Signal Changes ◽  
Sodium Regulation ◽  
Pcc 7120 ◽  
Camp And Cgmp

Cyclic nucleotide PDEs (phosphodiesterases) regulate cellular levels of cAMP and cGMP by controlling the rate of degradation. Several mammalian PDE isoforms possess N-terminal GAF (found in cGMP PDEs, Anabaena adenylate cyclases and Escherichia coli FhlA; where FhlA is formate hydrogen lyase transcriptional activator) domains that bind cyclic nucleotides. Similarly, the CyaB1 and CyaB2 ACs (adenylate cyclases) of the cyanobacterium Anabaena PCC 7120 bind cAMP through one (CyaB1) or two (CyaB2) N-terminal GAF domains and mediate autoregulation of the AC domain. Sodium inhibits the activity of CyaB1, CyaB2 and mammalian PDE2A in vitro through modulation of GAF domain function. Furthermore, genetic ablation of cyaB1 and cyaB2 gives rise to Anabaena strains defective in homoeostasis at limiting sodium. Sodium regulation of GAF domain function has therefore been conserved since the eukaryotic/prokaryotic divergence. The GAF domain is the first identified protein domain to directly sense and signal changes in environmental sodium.

Isolation and Sequence of the Gene for Ferredoxin I from the Cyanobacterium Anabaena PCC 7120

1987 ◽  
pp. 793-795 ◽  
Author(s):  
Jawed Alam ◽  
Richard A. Whitaker ◽  
David W. Krogmann ◽  
Stephanie E. Curtis
Keyword(s):  
Anabaena Pcc 7120 ◽  
Cyanobacterium Anabaena ◽  
Ferredoxin I ◽  
Pcc 7120

Functional and mechanistic insights into the differential effect of the toxicant ‘Se(IV)’ in the cyanobacterium Anabaena PCC 7120

2021 ◽  
pp. 105839
Author(s):  
Manisha Banerjee ◽  
Prakash Kalwani ◽  
Dhiman Chakravarty ◽  
Beena Singh ◽  
Anand Ballal
Keyword(s):  
Differential Effect ◽  
Anabaena Pcc 7120 ◽  
Cyanobacterium Anabaena ◽  
Pcc 7120

Synthesis of a Bicyclobutane Fatty Acid Identified from the Cyanobacterium Anabaena PCC 7120

2011 ◽  
Vol 123 (42) ◽  
pp. 10114-10116 ◽  
Author(s):  
Sean M. DeGuire ◽  
Shutao Ma ◽  
Gary A. Sulikowski
Keyword(s):  
Fatty Acid ◽  
Anabaena Pcc 7120 ◽  
Cyanobacterium Anabaena ◽  
Pcc 7120

scholarly journals RNase II binds to RNase E and modulates its endoribonucleolytic activity in the cyanobacterium Anabaena PCC 7120

2020 ◽  
Vol 48 (7) ◽  
pp. 3922-3934 ◽  
Author(s):  
Cong Zhou ◽  
Juyuan Zhang ◽  
Xinyu Hu ◽  
Changchang Li ◽  
Li Wang ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Bacterial Species ◽  
Rna Degradation ◽  
Rnase E ◽  
Anabaena Pcc 7120 ◽  
Cyanobacterium Anabaena ◽  
Rna Degradosome ◽  
Rnase Ii ◽  
Pcc 7120

Abstract In Escherichia coli, the endoribonuclease E (RNase E) can recruit several other ribonucleases and regulatory proteins via its noncatalytic domain to form an RNA degradosome that controls cellular RNA turnover. Similar RNA degradation complexes have been found in other bacteria; however, their compositions are varied among different bacterial species. In cyanobacteria, only the exoribonuclease PNPase was shown to bind to the noncatalytic domain of RNase E. Here, we showed that Alr1240, a member of the RNB family of exoribonucleases, could be co-isolated with RNase E from the lysate of the cyanobacterium Anabaena PCC 7120. Enzymatic analysis revealed that Alr1240 is an exoribonuclease II (RNase II), as it only degrades non-structured single-stranded RNA substrates. In contrast to known RNase E-interacting ribonucleases, which bind to the noncatalytic domain of RNase E, the Anabaena RNase II was shown to associate with the catalytic domain of RNase E. Using a strain in which RNase E and RNase II were tagged in situ with GFP and BFP, respectively, we showed that RNase E and RNase II form a compact complex in vivo by a fluorescence resonance energy transfer (FRET) assay. RNase E activity on several synthetic substrates was boosted in the presence of RNase II, suggesting that the activity of RNase E could be regulated by RNase II-RNase E interaction. To our knowledge, Anabaena RNase II is an unusual ribonuclease that interacts with the catalytic domain of RNase E, and it may represent a new type of RNA degradosome and a novel mechanism for regulating the activity of the RNA degradosome. As Anabaena RNase E interacts with RNase II and PNPase via different regions, it is very likely that the three ribonucleases form a large complex and cooperatively regulate RNA metabolism in the cell.

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