Identification of a novel heteroglycan-interacting protein, HIP 1.3, from Arabidopsis thaliana

Copyright © 2010 Elsevier GmbH. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Journal of plant physiology. - 1979. - 168(2011), 12 vom: 15. Aug., Seite 1415-25
1. Verfasser: Fettke, Joerg (VerfasserIn)
Weitere Verfasser: Nunes-Nesi, Adriano, Fernie, Alisdair R, Steup, Martin
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2011
Zugriff auf das übergeordnete Werk:Journal of plant physiology
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis Proteins Buffers Carrier Proteins HIP1.3 protein, Arabidopsis Monosaccharides Plant Extracts Polysaccharides Starch mehr... 9005-25-8 Phosphorylases EC 2.4.1.- PHS2 protein, Arabidopsis EC 2.4.1.1
LEADER 01000naa a22002652 4500
001 NLM203720466
003 DE-627
005 20231223230647.0
007 cr uuu---uuuuu
008 231223s2011 xx |||||o 00| ||eng c
024 7 |a 10.1016/j.jplph.2010.09.008  |2 doi 
028 5 2 |a pubmed24n0679.xml 
035 |a (DE-627)NLM203720466 
035 |a (NLM)21087810 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Fettke, Joerg  |e verfasserin  |4 aut 
245 1 0 |a Identification of a novel heteroglycan-interacting protein, HIP 1.3, from Arabidopsis thaliana 
264 1 |c 2011 
336 |a Text  |b txt  |2 rdacontent 
337 |a ƒaComputermedien  |b c  |2 rdamedia 
338 |a ƒa Online-Ressource  |b cr  |2 rdacarrier 
500 |a Date Completed 07.10.2011 
500 |a Date Revised 30.09.2020 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a Copyright © 2010 Elsevier GmbH. All rights reserved. 
520 |a Plastidial degradation of transitory starch yields mainly maltose and glucose. Following the export into the cytosol, maltose acts as donor for a glucosyl transfer to cytosolic heteroglycans as mediated by a cytosolic transglucosidase (DPE2; EC 2.4.1.25) and the second glucosyl residue is liberated as glucose. The cytosolic phosphorylase (Pho2/PHS2; EC 2.4.1.1) also interacts with heteroglycans using the same intramolecular sites as DPE2. Thus, the two glucosyl transferases interconnect the cytosolic pools of glucose and glucose 1-phosphate. Due to the complex monosaccharide pattern, other heteroglycan-interacting proteins (HIPs) are expected to exist. Identification of those proteins was approached by using two types of affinity chromatography. Heteroglycans from leaves of Arabidopsis thaliana (Col-0) covalently bound to Sepharose served as ligands that were reacted with a complex mixture of buffer-soluble proteins from Arabidopsis leaves. Binding proteins were eluted by sodium chloride. For identification, SDS-PAGE, tryptic digestion and MALDI-TOF analyses were applied. A strongly interacting polypeptide (approximately 40kDa; designated as HIP1.3) was observed as product of locus At1g09340. Arabidopsis mutants deficient in HIP1.3 were reduced in growth and contained heteroglycans displaying an altered monosaccharide pattern. Wild type plants express HIP1.3 most strongly in leaves. As revealed by immuno fluorescence, HIP1.3 is located in the cytosol of mesophyll cells but mostly associated with the cytosolic surface of the chloroplast envelope membranes. In an HIP1.3-deficient mutant the immunosignal was undetectable. Metabolic profiles from leaves of this mutant and wild type plants as well were determined by GC-MS. As compared to the wild type control, more than ten metabolites, such as ascorbic acid, fructose, fructose bisphosphate, glucose, glycine, were elevated in darkness but decreased in the light. Although the biochemical function of HIP1.3 has not yet been elucidated, it is likely to possess an important function in the central carbon metabolism of higher plants 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Buffers  |2 NLM 
650 7 |a Carrier Proteins  |2 NLM 
650 7 |a HIP1.3 protein, Arabidopsis  |2 NLM 
650 7 |a Monosaccharides  |2 NLM 
650 7 |a Plant Extracts  |2 NLM 
650 7 |a Polysaccharides  |2 NLM 
650 7 |a Starch  |2 NLM 
650 7 |a 9005-25-8  |2 NLM 
650 7 |a Phosphorylases  |2 NLM 
650 7 |a EC 2.4.1.-  |2 NLM 
650 7 |a PHS2 protein, Arabidopsis  |2 NLM 
650 7 |a EC 2.4.1.1  |2 NLM 
700 1 |a Nunes-Nesi, Adriano  |e verfasserin  |4 aut 
700 1 |a Fernie, Alisdair R  |e verfasserin  |4 aut 
700 1 |a Steup, Martin  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Journal of plant physiology  |d 1979  |g 168(2011), 12 vom: 15. Aug., Seite 1415-25  |w (DE-627)NLM098174622  |x 1618-1328  |7 nnns 
773 1 8 |g volume:168  |g year:2011  |g number:12  |g day:15  |g month:08  |g pages:1415-25 
856 4 0 |u http://dx.doi.org/10.1016/j.jplph.2010.09.008  |3 Volltext 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_350 
951 |a AR 
952 |d 168  |j 2011  |e 12  |b 15  |c 08  |h 1415-25