<scp>HesF</scp>, an exoprotein required for filament adhesion and aggregation in <scp><i>A</i></scp><i>nabaena</i> sp. <scp>PCC</scp> 7120

Oliveira, Paulo; Pinto, Filipe; Pacheco, Catarina C.; Mota, Rita; Tamagnini, Paula

doi:10.1111/1462-2920.12600

Cited by 30 publications

(25 citation statements)

References 67 publications

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“…The donor E. coli strain HB101 contained the conjugal plasmid pRL443 and the helper plasmid pRL623 (Elhai and Wolk, 1988; Elhai et al, 1997). To generate constructs for deletion of the rfpA, rfpB , or rfpC genes, an ermC cassette, which confers resistance to erythromycin, was amplified through PCR and cloned onto the cargo plasmid pRL277 using SacI and SphI restriction sites (see Table S1 for primer sequences).…”

Section: Methodsmentioning

confidence: 99%

RfpA, RfpB, and RfpC are the Master Control Elements of Far-Red Light Photoacclimation (FaRLiP)

et al. 2015

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Terrestrial cyanobacteria often occur in niches that are strongly enriched in far-red light (FRL; λ > 700 nm). Some cyanobacteria exhibit a complex and extensive photoacclimation response, known as FRL photoacclimation (FaRLiP). During the FaRLiP response, specialized paralogous proteins replace 17 core subunits of the three major photosynthetic complexes: Photosystem (PS) I, PS II, and the phycobilisome. Additionally, the cells synthesize both chlorophyll (Chl) f and Chl d. Using biparental mating from Escherichia coli, we constructed null mutants of three genes, rfpA, rfpB, and rfpC, in the cyanobacteria Chlorogloeopsis fritschii PCC 9212 and Chroococcidiopsis thermalis PCC 7203. The resulting mutants were no longer able to modify their photosynthetic apparatus to absorb FRL, were no longer able to synthesize Chl f, inappropriately synthesized Chl d in white light, and were unable to transcribe genes of the FaRLiP gene cluster. We conclude that RfpA, RfpB, and RfpC constitute a FRL-activated signal transduction cascade that is the master control switch for the FaRLiP response. FRL is proposed to activate (or inactivate) the histidine kinase activity of RfpA, which leads to formation of the active state of RfpB, the key response regulator and transcription activator. RfpC may act as a phosphate shuttle between RfpA and RfpB. Our results show that reverse genetics via conjugation will be a powerful approach in detailed studies of the FaRLiP response.

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Section: Methodsmentioning

confidence: 99%

RfpA, RfpB, and RfpC are the Master Control Elements of Far-Red Light Photoacclimation (FaRLiP)

et al. 2015

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“…For exoproteome isolation, the method described by Oliveira et al . () was followed. Concentrated exoproteome samples were either used immediately or stored at −20°C until further analysis.…”

Section: Methodsmentioning

confidence: 97%

Identification of inner membrane translocase components of TolC‐mediated secretion in the cyanobacterium Synechocystis sp. PCC 6803

Gonçalves

Pacheco

Tamagnini

et al. 2018

Environmental Microbiology

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Cyanobacteria were the first organisms ever to perform oxygenic photosynthesis and still significantly contribute to primary production on a global scale. To assure the proper functioning of their primary metabolism and cell homeostasis, cyanobacteria must rely on efficient transport systems to cross their multilayered cell envelope. However, cyanobacterial secretion mechanisms remain largely unknown. Here, we report on the identification of 11 putative inner membrane translocase components of TolC-mediated secretion in the unicellular cyanobacterium Synechocystis sp. PCC 6803. Gene-inactivation of each of the candidate genes followed by a comprehensive phenotypic characterization allowed to link specific protein components to the processes of protein export (as part of the type I secretion system) and drug efflux (part of the resistance-division-nodulation efflux pumps). In addition, mutants in genes sll0141, sll0180 and slr0369 exhibited alterations in pilin glycosylation, but pili structures could still be observed by transmission electron microscopy. By studying the release of outer membrane vesicles (OMVs), an alternative secretion route, on mutants with impaired secretory functions we suggest that the hyper-vesiculating phenotype of the TolC-deficient mutant is related to cell envelope stress management. Altogether, these findings highlight how both classical (TolC-mediated) and nonclassical (OMVs-mediated) secretion systems are crucial for cyanobacterial cell homeostasis.

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“…The exoprotein HesF of Anabaena sp. PCC 7120 is required for filament adhesion and aggregation (Oliveira et al, 2015), and the surface glycoprotein MrpC is implicated in cell-cell attachment in Microcystis aeruginosa PCC 7806 (Zilliges et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

A microcin processing peptidase‐like protein of the cyanobacterium Synechococcus elongatus is essential for secretion of biofilm‐promoting proteins

Parnasa

Sendersky

Simkovsky

et al. 2019

Environ Microbiol Rep

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Summary Small secreted compounds, e.g. microcins, are characterized by a double‐glycine (GG) secretion motif that is cleaved off upon maturation. Genomic analysis suggests that small proteins that possess a GG motif are widespread in cyanobacteria; however, the roles of these proteins are largely unknown. Using a biofilm‐proficient mutant of the cyanobacterium Synechococcus elongatus PCC 7942 in which the constitutive biofilm self‐suppression mechanism is inactivated, we previously demonstrated that four small proteins, Enable biofilm formation with a GG motif (EbfG1‐4), each with a GG motif, enable biofilm formation. Furthermore, a peptidase belonging to the C39 family, Peptidase transporter enabling Biofilm (PteB), is required for secretion of these proteins. Here, we show that the microcin processing peptidase‐like protein encoded by gene Synpcc7942_1127 is also required for biofilm development – inactivation of this gene in the biofilm‐proficient mutant abrogates biofilm development. Additionally, this peptidase‐like protein (denoted EbfE – enables biofilm formation peptidase) is required for secretion of the EbfG biofilm‐promoting small proteins. Given their protein‐domain characteristics, we suggest that PteB and EbfE take part in a maturation‐secretion system, with PteB being located to the cell membrane while EbfE is directed to the periplasmic space via its secretion signal.

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HesF, an exoprotein required for filament adhesion and aggregation in Anabaena sp. PCC 7120

Cited by 30 publications

References 67 publications

RfpA, RfpB, and RfpC are the Master Control Elements of Far-Red Light Photoacclimation (FaRLiP)

RfpA, RfpB, and RfpC are the Master Control Elements of Far-Red Light Photoacclimation (FaRLiP)

Identification of inner membrane translocase components of TolC‐mediated secretion in the cyanobacterium Synechocystis sp. PCC 6803

A microcin processing peptidase‐like protein of the cyanobacterium Synechococcus elongatus is essential for secretion of biofilm‐promoting proteins

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