Numerous posttranslational modifications provide opportunities for the intricate regulation of metabolic enzymes at multiple levels

被引:79
作者
Huber, SC [1 ]
Hardin, SC
机构
[1] USDA ARS, Photosynthesis Res Unit, Urbana, IL 61801 USA
[2] Univ Illinois, Dept Plant Biol, Urbana, IL 61801 USA
[3] Univ Illinois, Dept Crop Sci, Urbana, IL 61801 USA
关键词
D O I
10.1016/j.pbi.2004.03.002
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The metabolic plasticity displayed by plants during normal development, and in response to environmental fluctuations and stressors, is essential for their growth and survival. The capacity to regulate metabolic enzymes intricately arises in part from posttranslational modifications that can affect enzymatic activity, intracellular localization, protein-protein interactions, and stability. Protein phosphorylation and thiol/disulfide redox modulation are important modifications, in plants, and it is likely that O-glycosylation and S-nitrosylation will also emerge as important mechanisms. Recent advances in the field of proteomics, in particular the development of novel and specific chemistries for the detection of a diverse number of modifications, are rapidly expanding our awareness of possible modifications and our understanding of the enzymes whose functions are likely to be regulated posttranslationally.
引用
收藏
页码:318 / 322
页数:5
相关论文
共 36 条
  • [1] Activation of the potato tuber ADP-glucose pyrophosphorylase by thioredoxin
    Ballicora, MA
    Frueauf, JB
    Fu, YB
    Schürmann, P
    Preiss, J
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (02) : 1315 - 1320
  • [2] Proteomics gives insight into the regulatory function of chloroplast thioredoxins
    Balmer, Y
    Koller, A
    del Val, G
    Manieri, W
    Schürmann, P
    Buchanan, BB
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (01) : 370 - 375
  • [3] BALMER Y, 2004, IN PRESS PHOTOSYNTH
  • [4] RETRACTED: The pathogen-inducible nitric oxide synthase (iNOS) in plants is a variant of the P protein of the glycine decarboxylase complex (Retracted Article. See vol 119, pg 445, 2004)
    Chandok, MR
    Ytterberg, AJ
    van Wijk, KJ
    Klessig, DF
    [J]. CELL, 2003, 113 (04) : 469 - 482
  • [5] 14-3-3s regulate global cleavage of their diverse binding partners in sugar-starved Arabidopsis cells
    Cotelle, V
    Meek, SEM
    Provan, F
    Milne, FC
    Morrice, N
    MacKintosh, C
    [J]. EMBO JOURNAL, 2000, 19 (12) : 2869 - 2876
  • [6] Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins
    Elortza, F
    Nühse, TS
    Foster, LJ
    Stensballe, A
    Peck, SC
    Jensen, ON
    [J]. MOLECULAR & CELLULAR PROTEOMICS, 2003, 2 (12) : 1261 - 1270
  • [7] Mechanism of reductive activation of potato tuber ADP-glucose pyrophosphorylase
    Fu, YB
    Ballicora, MA
    Leykam, JF
    Preiss, J
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (39) : 25045 - 25052
  • [8] Phosphorylation of sucrose synthase at serine 170: occurrence and possible role as a signal for proteolysis
    Hardin, SC
    Tang, GQ
    Scholz, A
    Holtgraewe, D
    Winter, H
    Huber, SC
    [J]. PLANT JOURNAL, 2003, 35 (05) : 588 - 603
  • [9] HARDIN SC, 2004, IN PRESS PLANT PHYSL
  • [10] ADP-glucose pyrophosphorylase is activated by posttranslational redox-modification in response to light and to sugars in leaves of Arabidopsis and other plant species
    Hendriks, JHM
    Kolbe, A
    Gibon, Y
    Stitt, M
    Geigenberger, P
    [J]. PLANT PHYSIOLOGY, 2003, 133 (02) : 838 - 849