ArticleJournal of bacteriology1998
Molecular and genetic analysis of two closely linked genes that encode, respectively, a protein phosphatase 1/2A/2B homolog and a protein kinase homolog in the cyanobacterium Anabaena sp. strain PCC 7120.
Article in Journal of bacteriology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 61 citations in OpenAlex.
- R-DeeP/TripepSVM identifies the RNA-binding OB-fold-like protein PatR as regulator of heterocyst patterning.Nucleic acids research · 2025Article
- Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments.International journal of molecular sciences · 2018Review
- The composition of the global and feature specific cyanobacterial core-genomes.Frontiers in microbiology · 2015Article
- Global transcription profiles of the nitrogen stress response resulting in heterocyst or hormogonium development in Nostoc punctiforme.Journal of bacteriology · 2011Article
- Aspects of eukaryotic-like signaling in Gram-positive cocci: a focus on virulence.Future microbiology · 2011Review
- Overexpression of pknE blocks heterocyst development in Anabaena sp. strain PCC 7120.Journal of bacteriology · 2011Article
- Myxococcus xanthus Pph2 is a manganese-dependent protein phosphatase involved in energy metabolism.The Journal of biological chemistry · 2009Article
- Mutual regulation of ntcA and hetR during heterocyst differentiation requires two similar PP2C-type protein phosphatases, PrpJ1 and PrpJ2, in Anabaena sp. strain PCC 7120.Journal of bacteriology · 2009Article
- Genome-wide survey of putative serine/threonine protein kinases in cyanobacteria.BMC genomics · 2007Article
- Signal transduction genes required for heterocyst maturation in Anabaena sp. strain PCC 7120.Journal of bacteriology · 2006Article
- Role of Mycobacterium tuberculosis Ser/Thr kinase PknF: implications in glucose transport and cell division.Journal of bacteriology · 2005Article
- Identification of two eukaryote-like serine/threonine kinases encoded by Chlamydia trachomatis serovar L2 and characterization of interacting partners of Pkn1.Infection and immunity · 2003Article
- HstK, a cyanobacterial protein with both a serine/threonine kinase domain and a histidine kinase domain: implication for the mechanism of signal transduction.The Biochemical journal · 2001Article
- A PP2C-type phosphatase dephosphorylates the PII signaling protein in the cyanobacterium Synechocystis PCC 6803.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Expression and characterization of the Mycobacterium tuberculosis serine/threonine protein kinase PknB.Infection and immunity · 1999Article
- Characterization of a Hank's type serine/threonine kinase and serine/threonine phosphoprotein phosphatase in Pseudomonas aeruginosa.Journal of bacteriology · 1999Article
- Pkg2, a novel transmembrane protein Ser/Thr kinase of Streptomyces granaticolor.Journal of bacteriology · 1999Article
- Survey, analysis and genetic organization of genes encoding eukaryotic-like signaling proteins on a cyanobacterial genome.Nucleic acids research · 1998Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reversible protein phosphorylation plays important roles in signal transduction. One gene, prpA, encoding a protein similar to eukaryotic types of phosphoprotein phosphatases PP1, PP2A, and PP2B, was cloned from the nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120. Interestingly, a eukaryotic-type protein kinase gene, pknE, was found 301 bp downstream of prpA. This unusual genetic arrangement provides the opportunity for study about how the balance between protein phosphorylation and dephosphorylation can regulate cellular activities. Both proteins were overproduced in Escherichia coli and used to raise polyclonal antibodies. Immunodetection and RNA/DNA hybridization experiments suggest that these two genes are unlikely to be coexpressed, despite their close genetic linkage. PrpA is expressed constitutively under different nitrogen conditions, while PknE expression varies according to the nature of the nitrogen source. Inactivation analysis in vivo suggests that PrpA and PknE function to ensure a correct level of phosphorylation of the targets in order to regulate similar biological processes such as heterocyst structure formation and nitrogen fixation.
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