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Planta

, Volume 235, Issue 4, pp 851–861 | Cite as

Sucrose phosphate phosphatase in the green alga Klebsormidium flaccidum (Streptophyta) lacks an extensive C-terminal domain and differs from that of land plants

  • Manabu Nagao
  • Matsuo UemuraEmail author
Original Article

Abstract

Previously, it was reported that like land plants, the green alga Klebsormidium flaccidum (Streptophyta) accumulates sucrose during cold acclimation (Nagao et al. Plant Cell Environ 31:872–885, 2008), suggesting that synthesis of sucrose could enhance the freezing tolerance of this alga. Because sucrose phosphate phosphatase (SPP; EC 3.1.3.24) is a key enzyme in the sucrose synthesis pathway in plants, we analyzed the SPP gene in K. flaccidum (KfSPP, GenBank accession number AB669024) to clarify its role in sucrose accumulation. As determined from its deduced amino acid sequence, KfSPP contains the N-terminal domain that is characteristic of the L-2-haloacid-dehalogenase family of phosphatases/hydrolases (the HAD phosphatase domain). However, it lacks the extensive C-terminal domain found in SPPs of land plants. Database searches revealed that the SPPs in cyanobacteria also lack the C-terminal domain. In addition, the green alga Coccomyxa (Chlorophyta) and K. flaccidum, which are closely related to land plants, have cyanobacterial-type SPPs, while Chlorella (Chlorophyta) has a land plant-type SPP. These results demonstrate that even K. flaccidum (Streptophyta), as a recent ancestor of land plants, has the cyanobacterial-type SPP lacking the C-terminal domain. Because SPP and sucrose phosphate synthase (SPS) catalyze sequential reactions in sucrose synthesis in green plant cells and the lack of the C-terminal domain in KfSPP is predicted to decrease its activity, the interaction between decreased KfSPP activity and SPS activity may alter sucrose synthesis during cold acclimation in K. flaccidum.

Keywords

C-terminal domain Green algae Klebsormidium flaccidum Streptophyta Sucrose phosphate phosphatase Sucrose synthesis 

Abbreviations

cDNA

Complementary DNA

HAD

L-2-Haloacid-dehalogenase

MW

Molecular weight

pI

Isoelectric point

RACE

Rapid amplification of cDNA ends

qRT-PCR

Quantitative real-time reverse transcription polymerase chain reaction

SPP

Sucrose phosphate phosphatase

SPS

Sucrose phosphate synthase

Suc6P

Sucrose 6′-phosphate

Notes

Acknowledgments

This work was supported in part by Grants-in-Aid for the 21st Century COE Program (K-3) and Scientific Research (17380062) to M.U. from the Ministry of Education, Culture, Sports, Science and Technology of Japan, and the Iwate University President Fund to M.N.

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Copyright information

© Springer-Verlag 2011

Authors and Affiliations

  1. 1.Cryobiofrontier Research CenterIwate UniversityMoriokaJapan
  2. 2.National Agricultural Research Center for Hokkaido RegionSapporoJapan

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