Isolation and complementation of mutants of Anabaena sp. strain PCC 7120 unable to grow aerobically on dinitrogen

Wölk, C. Peter; Cai, Yuping; Cardemil, Liliana; Flores, Enrique; Höhn, Barbara; Murry, Marcia A.; Schmetterer, Georg; Schrautemeier, Bernhard; Wilson, Ronald W.

doi:10.1128/jb.170.3.1239-1244.1988

Cited by 137 publications

(73 citation statements)

References 25 publications

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“…When strains containing the petE promoter were being constructed, we used a modified BG11 or BG11 0 medium without copper sulfate, and precautions were taken to remove trace amounts of copper, as previously described (8). Conjugation was carried out as previously described (12,48). The antibiotics aztreonam and cefsulodin were purchased from ICN Biomedicals, Inc.…”

Section: Methodsmentioning

confidence: 99%

Inhibition of Cell Division Suppresses Heterocyst Development in Anabaena sp. Strain PCC 7120

et al. 2006

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When the filamentous cyanobacterium Anabaena PCC 7120 is exposed to combined nitrogen starvation, 5 to 10% of the cells along each filament at semiregular intervals differentiate into heterocysts specialized in nitrogen fixation. Heterocysts are terminally differentiated cells in which the major cell division protein FtsZ is undetectable. In this report, we provide molecular evidence indicating that cell division is necessary for heterocyst development. FtsZ, which is translationally fused to the green fluorescent protein (GFP) as a reporter, is found to form a ring structure at the mid-cell position. SulA from Escherichia coli inhibits the GTPase activity of FtsZ in vitro and prevents the formation of FtsZ rings when expressed in Anabaena PCC 7120. The expression of sulA arrests cell division and suppresses heterocyst differentiation completely. The antibiotic aztreonam, which is targeted to the FtsI protein necessary for septum formation, has similar effects on both cell division and heterocyst differentiation, although in this case, the FtsZ ring is still formed. Therefore, heterocyst differentiation is coupled to cell division but independent of the formation of the FtsZ ring. Consistently, once the inhibitory pressure of cell division is removed, cell division should take place first before heterocyst differentiation resumes at a normal frequency. The arrest of cell division does not affect the accumulation of 2-oxoglutarate, which triggers heterocyst differentiation. Consistently, a nonmetabolizable analogue of 2-oxoglutarate does not rescue the failure of heterocyst differentiation when cell division is blocked. These results suggest that the control of heterocyst differentiation by cell division is independent of the 2-oxoglutarate signal.

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Section: Methodsmentioning

confidence: 99%

Inhibition of Cell Division Suppresses Heterocyst Development in Anabaena sp. Strain PCC 7120

et al. 2006

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“…The plasmids pHGFP, pNiHGEC, and pNiECGH were introduced into the wild-type Anabaena PCC7120 by conjugation (Wolk et al 1988). The resulting strains were grown in liquid BG 11 medium to OD700 = 0.5.…”

Section: Copurification Of Protein(s) Associated With Anarnec From Anmentioning

confidence: 99%

RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region

Zhang

Deng

et al. 2014

RNA

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RNase E, a central component involved in bacterial RNA metabolism, usually has a highly conserved N-terminal catalytic domain but an extremely divergent C-terminal domain. While the C-terminal domain of RNase E in Escherichia coli recruits other components to form an RNA degradation complex, it is unknown if a similar function can be found for RNase E in other organisms due to the divergent feature of this domain. Here, we provide evidence showing that RNase E forms a complex with another essential ribonuclease-the polynucleotide phosphorylase (PNPase)-in cyanobacteria, a group of ecologically important and phylogenetically ancient organisms. Sequence alignment for all cyanobacterial RNase E proteins revealed several conserved and variable subregions in their noncatalytic domains. One such subregion, an extremely conserved nonapeptide (RRRRRRSSA) located near the very end of RNase E, serves as the PNPase recognition site in both the filamentous cyanobacterium Anabaena PCC7120 and the unicellular cyanobacterium Synechocystis PCC6803. These results indicate that RNase E and PNPase form a ribonuclease complex via a common mechanism in cyanobacteria. The PNPase-recognition motif in cyanobacterial RNase E is distinct from those previously identified in Proteobacteria, implying a mechanism of coevolution for PNPase and RNase E in different organisms.

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“…Three genes, hetA, hetB (later renamed hepA and hepB, respectively ; Ernst et al, 1992) and hepC, are required for the synthesis or stabilization of the polysaccharide layer (Wolk et al, 1988 ;Holland & Wolk, 1990 ;Zhu et al, 1998). HepA resembles ATP-binding transport proteins (Khudyakov & Wolk, 1997).…”

Section: Heterocyst Structurementioning

confidence: 99%

Tansley Review No. 107. Heterocyst and akinete differentiation in cyanobacteria

1999

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Isolation and complementation of mutants of Anabaena sp. strain PCC 7120 unable to grow aerobically on dinitrogen

Cited by 137 publications

References 25 publications

Inhibition of Cell Division Suppresses Heterocyst Development in Anabaena sp. Strain PCC 7120

Inhibition of Cell Division Suppresses Heterocyst Development in Anabaena sp. Strain PCC 7120

RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region

Tansley Review No. 107. Heterocyst and akinete differentiation in cyanobacteria

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