Functional Dependence between Septal Protein SepJ from Anabaena sp. Strain PCC 7120 and an Amino Acid ABC-Type Uptake Transporter

Escudero, Leticia; Mariscal, Vicente; Flores, Enrique

doi:10.1128/jb.00289-15

Cited by 14 publications

(15 citation statements)

References 54 publications

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“…While its physiological role is rather clear, i.e. to stimulate the uptake of the polar amino acids (Montesinos et al ., ; Escudero et al ., ), it is not apparent why specific genes are used in desiccation‐tolerant cyanobacteria and, altogether, why it is essential to take up polar amino acids during desiccation. Interestingly, there are indications for the presence of free amino acids in the BSC during desiccation (Baran et al ., ; Barger et al ., ).…”

Section: Resultsmentioning

confidence: 99%

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What distinguishes cyanobacteria able to revive after desiccation from those that cannot: the genome aspect

Murik

Oren

Shotland

et al. 2016

Environmental Microbiology

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Filamentous cyanobacteria are the main founders and primary producers in biological desert soil crusts (BSCs) and are likely equipped to cope with one of the harshest environmental conditions on earth including daily hydration/dehydration cycles, high irradiance and extreme temperatures. Here, we resolved and report on the genome sequence of Leptolyngbya ohadii, an important constituent of the BSC. Comparative genomics identified a set of genes present in desiccation-tolerant but not in dehydration-sensitive cyanobacteria. RT qPCR analyses showed that the transcript abundance of many of them is upregulated during desiccation in L. ohadii. In addition, we identified genes where the orthologs detected in desiccation-tolerant cyanobacteria differs substantially from that found in desiccation-sensitive cells. We present two examples, treS and fbpA (encoding trehalose synthase and fructose 1,6-bisphosphate aldolase respectively) where, in addition to the orthologs present in the desiccation-sensitive strains, the resistant cyanobacteria also possess genes with different predicted structures. We show that in both cases the two orthologs are transcribed during controlled dehydration of L. ohadii and discuss the genetic basis for the acclimation of cyanobacteria to the desiccation conditions in desert BSC.

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Section: Resultsmentioning

confidence: 99%

“…While its physiological role is rather clear, i.e. to stimulate the uptake of the polar amino acids (Montesinos et al, 1997;Escudero et al, 2015), it is not apparent why specific Fig. 3.…”

Section: Comparative Genomicsmentioning

confidence: 99%

What distinguishes cyanobacteria able to revive after desiccation from those that cannot: the genome aspect

Murik

Oren

Shotland

et al. 2016

Environmental Microbiology

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“…The N-II transporter was found to be widespread in cyanobacteria, being present in about 77 % of the test strains and about 76 % of the strains that produce cyanophycin. It was previously known that the N-II transporter is absent from Synechocystis [58,63,64] and present in S. elongatus [76], strains that produce and does not produce cyanophycin, respectively. In spite of the fact that a strict correlation between the presence of the N-II transporter and cyanophycin is not found, the wide distribution of this transporter in cyanobacteria may permit the uptake of aspartate that, when available together with arginine, could be utilized at least in part by the ornithine-ammonia cycle.…”

Section: Co-occurrence Of Cyanophycin Agre/puta and Arginine And Aspmentioning

confidence: 99%

Cyanophycin and arginine metabolism in cyanobacteria

2019

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Cyanobacteria are oxygenic phoautotrophs that can utilize inorganic nitrogen salts, atmospheric nitrogen and some amino acids such as arginine as nitrogen source. Under unbalanced growth in the presence of sufficient nitrogen, many cyanobacteria accumulate cyanophycin, a co-polymer of aspartate and arginine that serves as a nitrogen reservoir. Cyanophycin metabolism enzymes include cyanophycin synthetases, cyanophycinase and isoaspartyl dipeptidase, which splits aspartyl arginine released from cyanophycin by cyanophycinase into aspartate and arginine. The arginine catabolic pathway of cyanobacteria has been recently elucidated and consists of two bifunctional enzymes, arginine-guanidine removing enzyme (AgrE) and proline oxidase (PutA). This pathway makes available to metabolism the four nitrogen atoms of arginine, three as ammonia and one as glutamate. A variant of the pathway cycles ornithine (an intermediate in the AgrE-catalyzed reactions) back to arginine incorporating aspartate and, hence, recovering its nitrogen atom for metabolism. Many cyanobacteria also make use of this pathway to utilize arginine taken up from the outer medium through a high-affinity ABC transporter. An analysis of co-occurrence in cyanobacteria of the genes encoding enzymes of cyanophycin metabolism, arginine catabolism and the arginine and aspartate transporters indicates a strong correlation between the presence of cyanophycin and the AgrE/PutA pathway.

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“…Hence, GlsP and HepP may affect SepJ function by means of proteinprotein interactions. A functional dependence between SepJ and an ABC transporter for polar amino acids has also been described (46). These observations suggest that proper operation of SepJ and, hence, of the SepJ-related septal junctions requires interaction with other cytoplasmic membrane proteins.…”

Section: Discussionmentioning

confidence: 68%

Specific Glucoside Transporters Influence Septal Structure and Function in the Filamentous, Heterocyst-Forming Cyanobacterium Anabaena sp. Strain PCC 7120

et al. 2017

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When deprived of combined nitrogen, some filamentous cyanobacteria contain two cell types: vegetative cells that fix CO 2 through oxygenic photosynthesis and heterocysts that are specialized in N 2 fixation. In the diazotrophic filament, the vegetative cells provide the heterocysts with reduced carbon (mainly in the form of sucrose) and heterocysts provide the vegetative cells with combined nitrogen. Septal junctions traverse peptidoglycan through structures known as nanopores and appear to mediate intercellular molecular transfer that can be traced with fluorescent markers, including the sucrose analog esculin (a coumarin glucoside) that is incorporated into the cells. Uptake of esculin by the model heterocyst-forming cyanobacterium Anabaena sp. strain PCC 7120 was inhibited by the ␣-glucosides sucrose and maltose. Analysis of Anabaena mutants identified components of three glucoside transporters that move esculin into the cells: GlsC (Alr4781) and GlsP (All0261) are an ATP-binding subunit and a permease subunit of two different ABC transporters, respectively, and HepP (All1711) is a major facilitator superfamily (MFS) protein that was shown previously to be involved in formation of the heterocyst envelope. Transfer of fluorescent markers (especially calcein) between vegetative cells of Anabaena was impaired by mutation of glucoside transporter genes. GlsP and HepP interact in bacterial two-hybrid assays with the septal junction-related protein SepJ, and GlsC was found to be necessary for the formation of a normal number of septal peptidoglycan nanopores and for normal subcellular localization of SepJ. Therefore, beyond their possible role in nutrient uptake in Anabaena, glucoside transporters influence the structure and function of septal junctions.IMPORTANCE Heterocyst-forming cyanobacteria have the ability to perform oxygenic photosynthesis and to assimilate atmospheric CO 2 and N 2 . These organisms grow as filaments that fix these gases specifically in vegetative cells and heterocysts, respectively. For the filaments to grow, these types of cells exchange nutrients, including sucrose, which serves as a source of reducing power and of carbon skeletons for the heterocysts. Movement of sucrose between cells in the filament takes place through septal junctions and has been traced with a fluorescent sucrose analog, esculin, that can be taken up by the cells. Here, we identified ␣-glucoside transporters of Anabaena that mediate uptake of esculin and, notably, influence septal structure and the function of septal junctions.

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Functional Dependence between Septal Protein SepJ from Anabaena sp. Strain PCC 7120 and an Amino Acid ABC-Type Uptake Transporter

Cited by 14 publications

References 54 publications

What distinguishes cyanobacteria able to revive after desiccation from those that cannot: the genome aspect

What distinguishes cyanobacteria able to revive after desiccation from those that cannot: the genome aspect

Cyanophycin and arginine metabolism in cyanobacteria

Specific Glucoside Transporters Influence Septal Structure and Function in the Filamentous, Heterocyst-Forming Cyanobacterium Anabaena sp. Strain PCC 7120

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