An Increase in Apparent Affinity for Sucrose of Mung Bean Sucrose Synthase Is Caused by In Vitro Phosphorylation or Directed Mutagenesis of Ser11

Nakai, Tomoya; Konishi, Teruko; Zhang, Xiuqing; Chollet, Raymond; Tonouchi, Naoto; Tsuchida, Takayasu; Yoshinaga, Fumihiro; Mori, Hitoshi; Sakai, Fukumi; Hayashi, Takahisa

doi:10.1093/oxfordjournals.pcp.a029339

Cited by 64 publications

(60 citation statements)

References 19 publications

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“…Ser-11 in the SusA sequence is orthologous to Ser-15 in maize, implicated in PM binding (Winter et al, 1997;Hardin et al, 2004). Phosphorylation of this Ser has also been implicated in the reversal of PM binding in soybean (Glycine max) nodules (Zhang et al, 1999) and with determining kinetic properties of the enzyme in mung bean (Vigna radiata; Nakai et al, 1998). Truncation of the N terminus in SusC also results in a considerable increase in predicted hydrophobicity of this region of the protein compared with the SusA, -B, and -D proteins (data not shown).…”

Section: Discussion Susc Is a Novel Sus Isoform Abundant In Cotton Fimentioning

confidence: 99%

A Novel Isoform of Sucrose Synthase Is Targeted to the Cell Wall during Secondary Cell Wall Synthesis in Cotton Fiber

et al. 2011

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Sucrose (Suc) synthase (Sus) is the major enzyme of Suc breakdown for cellulose biosynthesis in cotton (Gossypium hirsutum) fiber, an important source of fiber for the textile industry. This study examines the tissue-specific expression, relative abundance, and temporal expression of various Sus transcripts and proteins present in cotton. A novel isoform of Sus (SusC) is identified that is expressed at high levels during secondary cell wall synthesis in fiber and is present in the cell wall fraction. The phylogenetic relationships of the deduced amino acid sequences indicate two ancestral groups of Sus proteins predating the divergence of monocots and dicots and that SusC sequences form a distinct branch in the phylogeny within the dicotspecific clade. The subcellular location of the Sus isoforms is determined, and it is proposed that cell wall-localized SusC may provide UDP-glucose for cellulose and callose synthesis from extracellular sugars.

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Section: Discussion Susc Is a Novel Sus Isoform Abundant In Cotton Fimentioning

confidence: 99%

A Novel Isoform of Sucrose Synthase Is Targeted to the Cell Wall during Secondary Cell Wall Synthesis in Cotton Fiber

et al. 2011

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“…Some substrates involved in carbon metabolism have been identified through in vitro phosphorylation, such as sucrose phosphate synthase in spinach, 31,32) sucrose synthase in soybean, 33,34) and phosphoenolpyruvate carboxylase in maize and soybean, 35) that CDPKs have important roles in the regulation of plant carbon metabolism. Sucrose contents and metabolism intensity are considered as limiting factors in the biosynthesis of natural rubber in H. brasiliensis.…”

Section: )mentioning

confidence: 99%

Molecular Characterization ofHbCDPK1, an Ethephon-Induced Calcium-Dependent Protein Kinase Gene ofHevea brasiliensis

Zhu

Chen

Chang

et al. 2010

Bioscience, Biotechnology, and Biochemistry

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“…Although UDP is generally considered to be the preferred nucleoside diphosphate for SUS, numerous studies have shown that ADP serves as an effective acceptor molecule to produce ADP-glucose (ADPG) (5)(6)(7)(8)(9)(10)(11)(12)(13)(14). SUS is highly regulated both at transcriptional and posttranslational levels (15)(16)(17)(18)(19)(20)(21), and plays a predominant role in the entry of carbon into metabolism in nonphotosynthetic cells, and in determining both sink strength and phloem loading (22)(23)(24)(25).…”

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Sucrose synthase activity in the sus1/sus2/sus3/sus4 Arabidopsis mutant is sufficient to support normal cellulose and starch production

Baroja‐Fernández

Muñoz

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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Sucrose synthase (SUS) catalyzes the reversible conversion of sucrose and a nucleoside diphosphate into the corresponding nucleoside diphosphate-glucose and fructose. In Arabidopsis , a multigene family encodes six SUS (SUS1-6) isoforms. The involvement of SUS in the synthesis of UDP-glucose and ADP-glucose linked to Arabidopsis cellulose and starch biosynthesis, respectively, has been questioned by Barratt et al. [(2009) Proc Natl Acad Sci USA 106:13124–13129], who showed that ( i ) SUS activity in wild type (WT) leaves is too low to account for normal rate of starch accumulation in Arabidopsis , and ( ii ) different organs of the sus1/sus2/sus3/sus4 SUS mutant impaired in SUS activity accumulate WT levels of ADP-glucose, UDP-glucose, cellulose and starch. However, these authors assayed SUS activity under unfavorable pH conditions for the reaction. By using favorable pH conditions for assaying SUS activity, in this work we show that SUS activity in the cleavage direction is sufficient to support normal rate of starch accumulation in WT leaves. We also demonstrate that sus1/sus2/sus3/sus4 leaves display WT SUS5 and SUS6 expression levels, whereas leaves of the sus5/sus6 mutant display WT SUS1 – 4 expression levels. Furthermore, we show that SUS activity in leaves and stems of the sus1/sus2/sus3/sus4 and sus5/sus6 plants is ∼85% of that of WT leaves, which can support normal cellulose and starch biosynthesis. The overall data disprove Barratt et al. (2009) claims, and are consistent with the possible involvement of SUS in cellulose and starch biosynthesis in Arabidopsis .

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An Increase in Apparent Affinity for Sucrose of Mung Bean Sucrose Synthase Is Caused by In Vitro Phosphorylation or Directed Mutagenesis of Ser11

Cited by 64 publications

References 19 publications

A Novel Isoform of Sucrose Synthase Is Targeted to the Cell Wall during Secondary Cell Wall Synthesis in Cotton Fiber

A Novel Isoform of Sucrose Synthase Is Targeted to the Cell Wall during Secondary Cell Wall Synthesis in Cotton Fiber

Molecular Characterization ofHbCDPK1, an Ethephon-Induced Calcium-Dependent Protein Kinase Gene ofHevea brasiliensis

Sucrose synthase activity in the sus1/sus2/sus3/sus4 Arabidopsis mutant is sufficient to support normal cellulose and starch production

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