PMID- 9237614
OWN - NLM
STAT- MEDLINE
DCOM- 19970903
LR  - 20231213
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 410
IP  - 2-3
DP  - 1997 Jun 30
TI  - Seryl-phosphorylation of soybean nodule sucrose synthase (nodulin-100) by a 
      Ca2+-dependent protein kinase.
PG  - 126-30
AB  - Sucrose synthase (SS; EC 2.4.1.13) was radiolabeled in situ by incubating 
      detached soybean nodules with 32Pi. Phosphoamino acid analysis indicated that SS 
      was phosphorylated on a serine residue(s). In-vitro phosphorylation of purified 
      nodule SS by desalted nodule extracts was Ca2+-dependent. This SS-kinase was 
      partially purified (approximately 2200-fold) from nodules harvested from 
      illuminated plants. The molecular mass of the SS-kinase was about 55,000 on a 
      Superdex 75 size-exclusion column or in a denaturing autophosphorylation gel. 
      With either purified nodule SS or Syntide 2 as substrate, exogenous calmodulin 
      and phosphatidylserine showed little or no effect on the in-vitro activity of 
      this partially purified protein kinase. However, its activity was inhibited by 
      W-7. The purified nodule SS-kinase (or CDPK) phosphorylated nodule PEP 
      carboxylase (PEPC; EC 4.1.1.31) in the presence of Ca2+. In contrast, a partially 
      purified nodule PEPC-kinase preparation was incapable of phosphorylating nodule 
      SS. Unlike nodule PEPC [Zhang et al. (1995) Plant Physiol. 108, 1561-1568], the 
      phosphorylation state of SS is not likely modulated in planta by photosynthate 
      supply from the shoots.
FAU - Zhang, X Q
AU  - Zhang XQ
AD  - Department of Biochemistry, University of Nebraska-Lincoln, George W. Beadle 
      Center, 68588-0664, USA.
FAU - Chollet, R
AU  - Chollet R
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Membrane Proteins)
RN  - 0 (Plant Proteins)
RN  - 0 (nodulin)
RN  - 452VLY9402 (Serine)
RN  - EC 2.4.1.- (Glucosyltransferases)
RN  - EC 2.4.1.13 (sucrose synthase)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.1.- (calcium-dependent protein kinase)
SB  - IM
MH  - Glucosyltransferases/chemistry/*metabolism
MH  - *Membrane Proteins
MH  - Phosphorylation
MH  - Plant Proteins/chemistry/*metabolism
MH  - Protein Kinases/*metabolism
MH  - Serine/metabolism
MH  - Glycine max/*enzymology
EDAT- 1997/06/30 00:00
MHDA- 1997/06/30 00:01
CRDT- 1997/06/30 00:00
PHST- 1997/06/30 00:00 [pubmed]
PHST- 1997/06/30 00:01 [medline]
PHST- 1997/06/30 00:00 [entrez]
AID - S0014-5793(97)00537-1 [pii]
AID - 10.1016/s0014-5793(97)00537-1 [doi]
PST - ppublish
SO  - FEBS Lett. 1997 Jun 30;410(2-3):126-30. doi: 10.1016/s0014-5793(97)00537-1.