β-amylase 1 (BAM1) degrades transitory starch to sustain proline biosynthesis during drought stress

© The Author 2016. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 67(2016), 6 vom: 10. März, Seite 1819-26
1. Verfasser: Zanella, Martina (VerfasserIn)
Weitere Verfasser: Borghi, Gian Luca, Pirone, Claudia, Thalmann, Matthias, Pazmino, Diana, Costa, Alex, Santelia, Diana, Trost, Paolo, Sparla, Francesca
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2016
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis drought osmolytes proline transitory starch. β-amylases Arabidopsis Proteins Polysaccharides mehr... Starch 9005-25-8 Proline 9DLQ4CIU6V BAM1 protein, Arabidopsis EC 2.7.11.1 Protein Serine-Threonine Kinases
LEADER 01000naa a22002652 4500
001 NLM256677719
003 DE-627
005 20231224181153.0
007 cr uuu---uuuuu
008 231224s2016 xx |||||o 00| ||eng c
024 7 |a 10.1093/jxb/erv572  |2 doi 
028 5 2 |a pubmed24n0855.xml 
035 |a (DE-627)NLM256677719 
035 |a (NLM)26792489 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Zanella, Martina  |e verfasserin  |4 aut 
245 1 0 |a β-amylase 1 (BAM1) degrades transitory starch to sustain proline biosynthesis during drought stress 
264 1 |c 2016 
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 13.12.2016 
500 |a Date Revised 08.04.2022 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a © The Author 2016. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com. 
520 |a During photosynthesis of higher plants, absorbed light energy is converted into chemical energy that, in part, is accumulated in the form of transitory starch within chloroplasts. In the following night, transitory starch is mobilized to sustain the heterotrophic metabolism of the plant. β-amylases are glucan hydrolases that cleave α-1,4-glycosidic bonds of starch and release maltose units from the non-reducing end of the polysaccharide chain. In Arabidopsis, nocturnal degradation of transitory starch involves mainly β-amylase-3 (BAM3). A second β-amylase isoform, β-amylase-1 (BAM1), is involved in diurnal starch degradation in guard cells, a process that sustains stomata opening. However, BAM1 also contributes to diurnal starch turnover in mesophyll cells under osmotic stress. With the aim of dissecting the role of β-amylases in osmotic stress responses in Arabidopsis, mutant plants lacking either BAM1 or BAM3 were subject to a mild (150mM mannitol) and prolonged (up to one week) osmotic stress. We show here that leaves of osmotically-stressed bam1 plants accumulated more starch and fewer soluble sugars than both wild-type and bam3 plants during the day. Moreover, bam1 mutants were impaired in proline accumulation and suffered from stronger lipid peroxidation, compared with both wild-type and bam3 plants. Taken together, these data strongly suggest that carbon skeletons deriving from BAM1 diurnal degradation of transitory starch support the biosynthesis of proline required to face the osmotic stress. We propose the transitory-starch/proline interplay as an interesting trait to be tackled by breeding technologies aimingto improve drought tolerance in relevant crops 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Arabidopsis 
650 4 |a drought 
650 4 |a osmolytes 
650 4 |a proline 
650 4 |a transitory starch. 
650 4 |a β-amylases 
650 7 |a Arabidopsis Proteins  |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 Proline  |2 NLM 
650 7 |a 9DLQ4CIU6V  |2 NLM 
650 7 |a BAM1 protein, Arabidopsis  |2 NLM 
650 7 |a EC 2.7.11.1  |2 NLM 
650 7 |a Protein Serine-Threonine Kinases  |2 NLM 
650 7 |a EC 2.7.11.1  |2 NLM 
700 1 |a Borghi, Gian Luca  |e verfasserin  |4 aut 
700 1 |a Pirone, Claudia  |e verfasserin  |4 aut 
700 1 |a Thalmann, Matthias  |e verfasserin  |4 aut 
700 1 |a Pazmino, Diana  |e verfasserin  |4 aut 
700 1 |a Costa, Alex  |e verfasserin  |4 aut 
700 1 |a Santelia, Diana  |e verfasserin  |4 aut 
700 1 |a Trost, Paolo  |e verfasserin  |4 aut 
700 1 |a Sparla, Francesca  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t Journal of experimental botany  |d 1985  |g 67(2016), 6 vom: 10. März, Seite 1819-26  |w (DE-627)NLM098182706  |x 1460-2431  |7 nnns 
773 1 8 |g volume:67  |g year:2016  |g number:6  |g day:10  |g month:03  |g pages:1819-26 
856 4 0 |u http://dx.doi.org/10.1093/jxb/erv572  |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 67  |j 2016  |e 6  |b 10  |c 03  |h 1819-26