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Photosystem II photochemistry and phycobiliprotein of the red algae Kappaphycus alvarezii and their implications for light adaptation.

Guan X, Wang J, Zhu J, Yao C, Liu J, Qin S, Jiang P - Biomed Res Int (2013)

Bottom Line: Based on the PBP gene sequences, K. alvarezii, together with other red algae, assembled faster and showed a closer relationship with LL-Prochlorococcus compared to HL-Prochlorococcus.However, loci conserved with HL-Prochlorococcus but divergent with LL-Prochlorococcus were also found.The diversities of PE and PC are proposed to have played some roles during the algal evolution and divergence of light adaption.

View Article: PubMed Central - PubMed

Affiliation: School of Ocean Sciences, China University of Geosciences, Beijing 100083, China.

ABSTRACT
Photosystem II photochemistry and phycobiliprotein (PBP) genes of red algae Kappaphycus alvarezii, raw material of κ -carrageenan used in food and pharmaceutical industries, were analyzed in this study. Minimum saturating irradiance (I k) of this algal species was less than 115 μmol m(-2) s(-1). Its actual PSII efficiency (yield II) increased when light intensity enhanced and decreased when light intensity reached 200 μmol m(-2) s(-1). Under dim light, yield II declined at first and then increased on the fourth day. Under high light, yield II retained a stable value. These results indicate that K. alvarezii is a low-light-adapted species but possesses regulative mechanisms in response to both excessive and deficient light. Based on the PBP gene sequences, K. alvarezii, together with other red algae, assembled faster and showed a closer relationship with LL-Prochlorococcus compared to HL-Prochlorococcus. Many amino acid loci in PBP sequences of K. alvarezii were conserved with those of LL-Prochlorococcus. However, loci conserved with HL-Prochlorococcus but divergent with LL-Prochlorococcus were also found. The diversities of PE and PC are proposed to have played some roles during the algal evolution and divergence of light adaption.

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Related in: MedlinePlus

Predicted structure model of PE β-subunit (a) and α-subunit (b) of Kappaphycus alvarezii. PDB-1b8dK and PDB-1liaB were chosen as the model templates, respectively.
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fig4: Predicted structure model of PE β-subunit (a) and α-subunit (b) of Kappaphycus alvarezii. PDB-1b8dK and PDB-1liaB were chosen as the model templates, respectively.

Mentions: Forty-eight amino acid loci conserved with LL-Prochlorococcus but diverged with HL-Prochlorococcus were mapped onto β-PE tertiary structure of K. alvarezii in blue color (Figure 4(a)). These loci distribute to the following six domains: (1) N-terminal 2-10aa domain is obviously conserved, including the loci 3D function of interaction of N-terminus of α- and β-subunits; (2) 65-81aa domain (except 67I, 68A, 72N, 75T, 76N, and 79M) is adjacent to the motif of chromophore interaction; (3) 92-100aa domain (including 92Y, 94S, 96A, 98L, 99A, and 100G), in which 91R, 95Y are functions of α- and β-interaction and 100G is at the end of helix E; (4) 107-115aa domain (including 107D, 108R, 111N, 112G, and 115E) includes the functional loci 108R, 115E, and 116T (function of the possible linker interaction) and 112G (bend between helices F′ and F); (5) 130-140aa domain, in which loci 130A, 133I, 135 K, 139V, and 140A are located at the eighth helix (124-143aa); (6) C-terminal 167-172aa domain in which loci 172V, 170D, 168Y, and 167S are functions of possible interaction and; (7) 164E involved trimer-trimer interaction of hexamer formation. There were only four loci (K28, I60, T75, and L161) of β-PE polypeptide sequences similar to HL-Prochlorococcus  β-PE but different from LL-Prochlorococcus.


Photosystem II photochemistry and phycobiliprotein of the red algae Kappaphycus alvarezii and their implications for light adaptation.

Guan X, Wang J, Zhu J, Yao C, Liu J, Qin S, Jiang P - Biomed Res Int (2013)

Predicted structure model of PE β-subunit (a) and α-subunit (b) of Kappaphycus alvarezii. PDB-1b8dK and PDB-1liaB were chosen as the model templates, respectively.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3860078&req=5

fig4: Predicted structure model of PE β-subunit (a) and α-subunit (b) of Kappaphycus alvarezii. PDB-1b8dK and PDB-1liaB were chosen as the model templates, respectively.
Mentions: Forty-eight amino acid loci conserved with LL-Prochlorococcus but diverged with HL-Prochlorococcus were mapped onto β-PE tertiary structure of K. alvarezii in blue color (Figure 4(a)). These loci distribute to the following six domains: (1) N-terminal 2-10aa domain is obviously conserved, including the loci 3D function of interaction of N-terminus of α- and β-subunits; (2) 65-81aa domain (except 67I, 68A, 72N, 75T, 76N, and 79M) is adjacent to the motif of chromophore interaction; (3) 92-100aa domain (including 92Y, 94S, 96A, 98L, 99A, and 100G), in which 91R, 95Y are functions of α- and β-interaction and 100G is at the end of helix E; (4) 107-115aa domain (including 107D, 108R, 111N, 112G, and 115E) includes the functional loci 108R, 115E, and 116T (function of the possible linker interaction) and 112G (bend between helices F′ and F); (5) 130-140aa domain, in which loci 130A, 133I, 135 K, 139V, and 140A are located at the eighth helix (124-143aa); (6) C-terminal 167-172aa domain in which loci 172V, 170D, 168Y, and 167S are functions of possible interaction and; (7) 164E involved trimer-trimer interaction of hexamer formation. There were only four loci (K28, I60, T75, and L161) of β-PE polypeptide sequences similar to HL-Prochlorococcus  β-PE but different from LL-Prochlorococcus.

Bottom Line: Based on the PBP gene sequences, K. alvarezii, together with other red algae, assembled faster and showed a closer relationship with LL-Prochlorococcus compared to HL-Prochlorococcus.However, loci conserved with HL-Prochlorococcus but divergent with LL-Prochlorococcus were also found.The diversities of PE and PC are proposed to have played some roles during the algal evolution and divergence of light adaption.

View Article: PubMed Central - PubMed

Affiliation: School of Ocean Sciences, China University of Geosciences, Beijing 100083, China.

ABSTRACT
Photosystem II photochemistry and phycobiliprotein (PBP) genes of red algae Kappaphycus alvarezii, raw material of κ -carrageenan used in food and pharmaceutical industries, were analyzed in this study. Minimum saturating irradiance (I k) of this algal species was less than 115 μmol m(-2) s(-1). Its actual PSII efficiency (yield II) increased when light intensity enhanced and decreased when light intensity reached 200 μmol m(-2) s(-1). Under dim light, yield II declined at first and then increased on the fourth day. Under high light, yield II retained a stable value. These results indicate that K. alvarezii is a low-light-adapted species but possesses regulative mechanisms in response to both excessive and deficient light. Based on the PBP gene sequences, K. alvarezii, together with other red algae, assembled faster and showed a closer relationship with LL-Prochlorococcus compared to HL-Prochlorococcus. Many amino acid loci in PBP sequences of K. alvarezii were conserved with those of LL-Prochlorococcus. However, loci conserved with HL-Prochlorococcus but divergent with LL-Prochlorococcus were also found. The diversities of PE and PC are proposed to have played some roles during the algal evolution and divergence of light adaption.

Show MeSH
Related in: MedlinePlus