14-3-3 proteins control proteolysis of nitrate reductase in spinach leaves

被引：69

作者：

Weiner, H ^{[1
]}

Kaiser, WM ^{[1
]}

机构：

[1] Julius von Sachs Inst Biowissensch, Lehrstuhl Bot 1, D-97082 Wurzburg, Germany

来源：

FEBS LETTERS | 1999年 / 455卷 / 1-2期

关键词：

14-3-3; protein; nitrate reductase; protein turnover rate; protein : protein interaction; protein phosphorylation;

D O I：

10.1016/S0014-5793(99)00868-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

To test a possible role of 14-3-3 proteins in I he degradation of nitrate reductase (NR) in leaves, we monitored 14-3-3s bound to NR in leaf extracts. The amount of 14-3-3s that coimmunoprecipitated with serine 543 phospo-NR (p-NR) increased upon a light/dark transition. This was accompanied by a similar increase in the protein turnover rate of NR in leaves. Purified NR was degraded in extracts from darkened but not from illuminated leaves. Removal of 14-3-3s from such extracts prevented NR degradation. We conclude that the availability of 14-3-3s for p-NR regulates the stability of NR, (C) 1999 Federation of European Biochemical Societies.

引用

页码：75 / 78

页数：4

共 25 条

[1] 14-3-3 PROTEINS - A HIGHLY CONSERVED, WIDESPREAD FAMILY OF EUKARYOTIC PROTEINS [J].

AITKEN, A ;

COLLINGE, DB ;

VANHEUSDEN, BPH ;

ISOBE, T ;

ROSEBOOM, PH ;

ROSENFELD, G ;

SOLL, J .

TRENDS IN BIOCHEMICAL SCIENCES, 1992, 17 (12) :498-501

[2]

[Anonymous], 1988, Antibodies: A Laboratory Manual

[3] The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 protein [J].

Bachmann, M ;

Huber, JL ;

Liao, PC ;

Gage, DA ;

Huber, SC .

FEBS LETTERS, 1996, 387 (2-3) :127-131

[4] Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors [J].

Bogyo, M ;

McMaster, JS ;

Gaczynska, M ;

Tortorella, D ;

Goldberg, AL ;

Ploegh, H .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (13) :6629-6634

[5] CENTRAL OF I-KAPPA-B-ALPHA PROTEOLYSIS BY SITE-SPECIFIC, SIGNAL-INDUCED PHOSPHORYLATION [J].

BROWN, K ;

GERSTBERGER, S ;

CARLSON, L ;

FRANZOSO, G ;

SIEBENLIST, U .

SCIENCE, 1995, 267 (5203) :1485-1488

[6] NITRATE - NUTRIENT AND SIGNAL FOR PLANT-GROWTH [J].

CRAWFORD, NM .

PLANT CELL, 1995, 7 (07) :859-868

[7] Structure and sites of phosphorylation of 14-3-3 protein: Role in coordinating signal transduction pathways [J].

Dubois, T ;

Howell, S ;

Amess, B ;

Kerai, P ;

Learmonth, M ;

Madrazo, J ;

Chaudhri, M ;

Rittinger, K ;

Scarabel, M ;

Soneji, Y ;

Aitken, A .

JOURNAL OF PROTEIN CHEMISTRY, 1997, 16 (05) :513-522

[8] REVERSIBLE LIGHT DARK MODULATION OF SPINACH LEAF NITRATE REDUCTASE-ACTIVITY INVOLVES PROTEIN-PHOSPHORYLATION [J].

HUBER, JL ;

HUBER, SC ;

CAMPBELL, WH ;

REDINBAUGH, MG .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1992, 296 (01) :58-65

[9] ISOFORMS OF 14-3-3-PROTEIN CAN FORM HOMODIMERS AND HETERODIMERS IN-VIVO AND IN-VITRO - IMPLICATIONS FOR FUNCTION AS ADAPTER PROTEINS [J].

JONES, DH ;

LEY, S ;

AITKEN, A .

FEBS LETTERS, 1995, 368 (01) :55-58

[10] Correlation between apparent activation state of nitrate reductase (NR), NR hysteresis and degradation of NR protein [J].

Kaiser, WM ;

Huber, SC .

JOURNAL OF EXPERIMENTAL BOTANY, 1997, 48 (312) :1367-1374

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