Exploring the size limit of protein diffusion through the periplasm in cyanobacterium Anabaena sp. PCC 7120 using the 13 kDa iLOV fluorescent protein

Zhang, Lichen; Risoul, Véronique; Latifi, Amel; Christie, John M.; Zhang, Chengcai

doi:10.1016/j.resmic.2013.05.004

Cited by 18 publications

(19 citation statements)

References 51 publications

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“…PCC7120 was used as template. The PCR product, digested with BamHI and NheI, was cloned into pRL25N (37) digested with the same enzymes, yielding pRCG. The plasmid was sequenced to verify the fidelity of the PCR.…”

Section: Methodsmentioning

confidence: 99%

Requirement of Fra proteins for communication channels between cells in the filamentous nitrogen-fixing cyanobacteriumAnabaenasp. PCC 7120

Omairi-Nasser

Mariscal

Austin

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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The filamentous nitrogen-fixing cyanobacterium Anabaena sp. PCC 7120 differentiates specialized cells, heterocysts, that fix atmospheric nitrogen and transfer the fixed nitrogen to adjacent vegetative cells. Reciprocally, vegetative cells transfer fixed carbon to heterocysts. Several routes have been described for metabolite exchange within the filament, one of which involves communicating channels that penetrate the septum between adjacent cells. Several fra gene mutants were isolated 25 y ago on the basis of their phenotypes: inability to fix nitrogen and fragmentation of filaments upon transfer from N+ to N− media. Cryopreservation combined with electron tomography were used to investigate the role of three fra gene products in channel formation. FraC and FraG are clearly involved in channel formation, whereas FraD has a minor part. Additionally, FraG was located close to the cytoplasmic membrane and in the heterocyst neck, using immunogold labeling with antibody raised to the N-terminal domain of the FraG protein.

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Section: Methodsmentioning

confidence: 99%

Requirement of Fra proteins for communication channels between cells in the filamentous nitrogen-fixing cyanobacteriumAnabaenasp. PCC 7120

Omairi-Nasser

Mariscal

Austin

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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“…First, the nsrSR cluster together with the promoter of nsrB from Synechocystis PCC6803 were amplified using the oligonucleotides Psll0798R1541 and Psll0797F124m. Then, the PCR fragment was cloned into the E. coli-Anabaena shuttle vector pRL25N (Zhang et al 2013) with BamHI and XhoI, generating the plasmid pRLNi. Subsequently, the gfp-encoding region from p8760 was amplified using the oligonucleotides of PgfpF14 and pgfpR754a, digested with SalI and NotI, and ligated into pRLNi linearized with XhoI and NotI, resulting in the plasmid pRLNiHG.…”

Section: Plasmid Constructionmentioning

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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“…There are two plausible routes by which molecules might move from cell to cell (Haselkorn, 2008). Firstly, the periplasm of the filament appears to form a continuous compartment , albeit with some diffusion barriers to macromolecules (Zhang et al, 2013). Molecules could be exported from the cytoplasm to the periplasm, could diffuse through the continuous periplasm and be reimported across the cytoplasmic membrane into other cells (Flores et al, 2006).…”

Section: Cell-cell Communication In Filamentous Cyanobacteriamentioning

confidence: 99%

“…An important functional question that remains to be answered is the upper size limit for molecular movement through the septal junctions. Calcein, a fluorescent dye with a molecular weight of 623 Da, can diffuse from cell to cell through the channels (Mullineaux et al, 2008) but both green fluorescent protein (GFP) (27 kDa) and iLOV (13 kDa) are trapped in the cells in which they were produced (Yoon and Golden, 1998;Zhang et al, 2013). Therefore, the size limit must lie somewhere between 623 Da and 13 kDa, but more precise information is lacking.…”

Section: Cell-cell Communication In Filamentous Cyanobacteriamentioning

confidence: 99%

Tracing the path of a prokaryotic paracrine signal

Mullineaux

Nürnberg

2014

Molecular Microbiology

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Exploring the size limit of protein diffusion through the periplasm in cyanobacterium Anabaena sp. PCC 7120 using the 13 kDa iLOV fluorescent protein

Cited by 18 publications

References 51 publications

Requirement of Fra proteins for communication channels between cells in the filamentous nitrogen-fixing cyanobacteriumAnabaenasp. PCC 7120

Requirement of Fra proteins for communication channels between cells in the filamentous nitrogen-fixing cyanobacteriumAnabaenasp. PCC 7120

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

Tracing the path of a prokaryotic paracrine signal

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