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Sucrose in cyanobacteria: from a salt-response molecule to play a key role in nitrogen fixation.

Kolman MA, Nishi CN, Perez-Cenci M, Salerno GL - Life (Basel) (2015)

Bottom Line: In those prokaryotes, sucrose accumulation has been associated with salt acclimation, and considered as a compatible solute in low-salt tolerant strains.In the last years, functional characterizations of sucrose metabolizing enzymes, metabolic control analysis, cellular localization of gene expressions, and reverse genetic experiments have revealed that sucrose metabolism is crucial in the diazotrophic growth of heterocystic strains, and besides, that it can be connected to glycogen synthesis.This article briefly summarizes the current state of knowledge of sucrose physiological functions in modern cyanobacteria and how they might have evolved taking into account the phylogenetic analyses of sucrose enzymes.

View Article: PubMed Central - PubMed

Affiliation: Instituto de Investigaciones en Biodiversidad y Biotecnología (INBIOTEC-CONICET) and Fundación para Investigaciones Biológicas Aplicadas (FIBA), Mar del Plata B7600DHN, Argentina. mkolman@fiba.org.ar.

ABSTRACT
In the biosphere, sucrose is mainly synthesized in oxygenic photosynthetic organisms, such as cyanobacteria, green algae and land plants, as part of the carbon dioxide assimilation pathway. Even though its central position in the functional biology of plants is well documented, much less is known about the role of sucrose in cyanobacteria. In those prokaryotes, sucrose accumulation has been associated with salt acclimation, and considered as a compatible solute in low-salt tolerant strains. In the last years, functional characterizations of sucrose metabolizing enzymes, metabolic control analysis, cellular localization of gene expressions, and reverse genetic experiments have revealed that sucrose metabolism is crucial in the diazotrophic growth of heterocystic strains, and besides, that it can be connected to glycogen synthesis. This article briefly summarizes the current state of knowledge of sucrose physiological functions in modern cyanobacteria and how they might have evolved taking into account the phylogenetic analyses of sucrose enzymes.

No MeSH data available.


Domainal arrangements of sucrose-synthesis related proteins. SPS, SPP and SuS (sucrose-synthesis related proteins) are modular proteins based on a glycosyltransferase domain (GTD, red box) and a phosphohydrolase domain (PHD, green box) [9,19]. (A) Two domain arrangements have been described for cyanobacterial SPSs: (1) the minimal SPS unit (GTD), or unidomainal SPS; and (2) the two-domain SPS prototype (GTD-PHD) or bidomainal SPS; (B) SuS presents a GTD, with a characteristic N-terminal extension (yellow box). The resolution of the crystallographic structure of Halothermothrix orenii SPS (2r66A and 2r68A) [24], and of Arabidopsis thaliana SuS1 (3s28A) [25] allowed the identification of the residues involved in the sugar and in the NDP-glucose binding sites, within motif I and II, respectively (denoted with asterisks); (C) SPPs exhibit only a PHD. Motives III to V are characteristic of proteins grouped in the phosphohrydrolase superfamily and related to SPP activity. The crystallization Synechocystis sp. PCC 6803 SPP (1s2oA) led to the identification of the residues involved in the catalytic activity [26]. The critical residues were found within PHD motives (denoted with asterisks). Logos were constructed using the above mentioned conserved motives (WebLogo server [27]).
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life-05-00102-f002: Domainal arrangements of sucrose-synthesis related proteins. SPS, SPP and SuS (sucrose-synthesis related proteins) are modular proteins based on a glycosyltransferase domain (GTD, red box) and a phosphohydrolase domain (PHD, green box) [9,19]. (A) Two domain arrangements have been described for cyanobacterial SPSs: (1) the minimal SPS unit (GTD), or unidomainal SPS; and (2) the two-domain SPS prototype (GTD-PHD) or bidomainal SPS; (B) SuS presents a GTD, with a characteristic N-terminal extension (yellow box). The resolution of the crystallographic structure of Halothermothrix orenii SPS (2r66A and 2r68A) [24], and of Arabidopsis thaliana SuS1 (3s28A) [25] allowed the identification of the residues involved in the sugar and in the NDP-glucose binding sites, within motif I and II, respectively (denoted with asterisks); (C) SPPs exhibit only a PHD. Motives III to V are characteristic of proteins grouped in the phosphohrydrolase superfamily and related to SPP activity. The crystallization Synechocystis sp. PCC 6803 SPP (1s2oA) led to the identification of the residues involved in the catalytic activity [26]. The critical residues were found within PHD motives (denoted with asterisks). Logos were constructed using the above mentioned conserved motives (WebLogo server [27]).

Mentions: The functional characterization of the genes related to sucrose biosynthesis in unicellular and filamentous heterocyst-forming cyanobacteria have contributed to new insights into their structure, disclosing that SPS, SPP and SuS have a modular architecture [9]. The analysis of the two SPSs of Anabaena sp. PCC 7120 (SPS-A and SPS-B) uncovered an approximately 400 amino-acid region shared by all SPSs, allowing to define a functional glucosyltransferase domain (GTD) [19] (Figure 2). Similarly, the Anabaena SPP characterization [19] defined a phosphohydrolase domain (PHD) sharing conserved residues with other phosphohydrolases (Figure 2). SPSs support modularity since two different SPS domainal arrangements could be identified: the minimal SPS unit (GTD), coincidental with Anabaena SPSs, and the bidomainal SPS prototype (GTD-PHD), present in Synechocystis SPS, where the PHD is non-functional [19]. Additionally, the existence of bidomainal/bifunctional SPSs (exhibiting SPS and SPP activity) was demonstrated [12]. On the other hand, the analysis of SuS sequences also revealed that these proteins featured a GTD with a distinctive C-terminal extension [9].


Sucrose in cyanobacteria: from a salt-response molecule to play a key role in nitrogen fixation.

Kolman MA, Nishi CN, Perez-Cenci M, Salerno GL - Life (Basel) (2015)

Domainal arrangements of sucrose-synthesis related proteins. SPS, SPP and SuS (sucrose-synthesis related proteins) are modular proteins based on a glycosyltransferase domain (GTD, red box) and a phosphohydrolase domain (PHD, green box) [9,19]. (A) Two domain arrangements have been described for cyanobacterial SPSs: (1) the minimal SPS unit (GTD), or unidomainal SPS; and (2) the two-domain SPS prototype (GTD-PHD) or bidomainal SPS; (B) SuS presents a GTD, with a characteristic N-terminal extension (yellow box). The resolution of the crystallographic structure of Halothermothrix orenii SPS (2r66A and 2r68A) [24], and of Arabidopsis thaliana SuS1 (3s28A) [25] allowed the identification of the residues involved in the sugar and in the NDP-glucose binding sites, within motif I and II, respectively (denoted with asterisks); (C) SPPs exhibit only a PHD. Motives III to V are characteristic of proteins grouped in the phosphohrydrolase superfamily and related to SPP activity. The crystallization Synechocystis sp. PCC 6803 SPP (1s2oA) led to the identification of the residues involved in the catalytic activity [26]. The critical residues were found within PHD motives (denoted with asterisks). Logos were constructed using the above mentioned conserved motives (WebLogo server [27]).
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4390843&req=5

life-05-00102-f002: Domainal arrangements of sucrose-synthesis related proteins. SPS, SPP and SuS (sucrose-synthesis related proteins) are modular proteins based on a glycosyltransferase domain (GTD, red box) and a phosphohydrolase domain (PHD, green box) [9,19]. (A) Two domain arrangements have been described for cyanobacterial SPSs: (1) the minimal SPS unit (GTD), or unidomainal SPS; and (2) the two-domain SPS prototype (GTD-PHD) or bidomainal SPS; (B) SuS presents a GTD, with a characteristic N-terminal extension (yellow box). The resolution of the crystallographic structure of Halothermothrix orenii SPS (2r66A and 2r68A) [24], and of Arabidopsis thaliana SuS1 (3s28A) [25] allowed the identification of the residues involved in the sugar and in the NDP-glucose binding sites, within motif I and II, respectively (denoted with asterisks); (C) SPPs exhibit only a PHD. Motives III to V are characteristic of proteins grouped in the phosphohrydrolase superfamily and related to SPP activity. The crystallization Synechocystis sp. PCC 6803 SPP (1s2oA) led to the identification of the residues involved in the catalytic activity [26]. The critical residues were found within PHD motives (denoted with asterisks). Logos were constructed using the above mentioned conserved motives (WebLogo server [27]).
Mentions: The functional characterization of the genes related to sucrose biosynthesis in unicellular and filamentous heterocyst-forming cyanobacteria have contributed to new insights into their structure, disclosing that SPS, SPP and SuS have a modular architecture [9]. The analysis of the two SPSs of Anabaena sp. PCC 7120 (SPS-A and SPS-B) uncovered an approximately 400 amino-acid region shared by all SPSs, allowing to define a functional glucosyltransferase domain (GTD) [19] (Figure 2). Similarly, the Anabaena SPP characterization [19] defined a phosphohydrolase domain (PHD) sharing conserved residues with other phosphohydrolases (Figure 2). SPSs support modularity since two different SPS domainal arrangements could be identified: the minimal SPS unit (GTD), coincidental with Anabaena SPSs, and the bidomainal SPS prototype (GTD-PHD), present in Synechocystis SPS, where the PHD is non-functional [19]. Additionally, the existence of bidomainal/bifunctional SPSs (exhibiting SPS and SPP activity) was demonstrated [12]. On the other hand, the analysis of SuS sequences also revealed that these proteins featured a GTD with a distinctive C-terminal extension [9].

Bottom Line: In those prokaryotes, sucrose accumulation has been associated with salt acclimation, and considered as a compatible solute in low-salt tolerant strains.In the last years, functional characterizations of sucrose metabolizing enzymes, metabolic control analysis, cellular localization of gene expressions, and reverse genetic experiments have revealed that sucrose metabolism is crucial in the diazotrophic growth of heterocystic strains, and besides, that it can be connected to glycogen synthesis.This article briefly summarizes the current state of knowledge of sucrose physiological functions in modern cyanobacteria and how they might have evolved taking into account the phylogenetic analyses of sucrose enzymes.

View Article: PubMed Central - PubMed

Affiliation: Instituto de Investigaciones en Biodiversidad y Biotecnología (INBIOTEC-CONICET) and Fundación para Investigaciones Biológicas Aplicadas (FIBA), Mar del Plata B7600DHN, Argentina. mkolman@fiba.org.ar.

ABSTRACT
In the biosphere, sucrose is mainly synthesized in oxygenic photosynthetic organisms, such as cyanobacteria, green algae and land plants, as part of the carbon dioxide assimilation pathway. Even though its central position in the functional biology of plants is well documented, much less is known about the role of sucrose in cyanobacteria. In those prokaryotes, sucrose accumulation has been associated with salt acclimation, and considered as a compatible solute in low-salt tolerant strains. In the last years, functional characterizations of sucrose metabolizing enzymes, metabolic control analysis, cellular localization of gene expressions, and reverse genetic experiments have revealed that sucrose metabolism is crucial in the diazotrophic growth of heterocystic strains, and besides, that it can be connected to glycogen synthesis. This article briefly summarizes the current state of knowledge of sucrose physiological functions in modern cyanobacteria and how they might have evolved taking into account the phylogenetic analyses of sucrose enzymes.

No MeSH data available.