Histone deacetylase AtSRT2 regulates salt tolerance during seed germination via repression of vesicle-associated membrane protein 714 (VAMP714) in Arabidopsis

© 2022 The Authors. New Phytologist © 2022 New Phytologist Foundation.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 234(2022), 4 vom: 28. Mai, Seite 1278-1293
1. Verfasser: Tang, Wen-Si (VerfasserIn)
Weitere Verfasser: Zhong, Li, Ding, Qing-Qian, Dou, Yi-Ning, Li, Wei-Wei, Xu, Zhao-Shi, Zhou, Yong-Bin, Chen, Jun, Chen, Ming, Ma, You-Zhi
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2022
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis histone deacetylase salt stress seed germination sirtuin-like protein vesicle trafficking Arabidopsis Proteins Histones mehr... R-SNARE Proteins Hydrogen Peroxide BBX060AN9V SRT2 protein, Arabidopsis EC 3.5.1.- Sirtuins Histone Deacetylases EC 3.5.1.98
LEADER 01000naa a22002652 4500
001 NLM337561958
003 DE-627
005 20231225234710.0
007 cr uuu---uuuuu
008 231225s2022 xx |||||o 00| ||eng c
024 7 |a 10.1111/nph.18060  |2 doi 
028 5 2 |a pubmed24n1125.xml 
035 |a (DE-627)NLM337561958 
035 |a (NLM)35224735 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Tang, Wen-Si  |e verfasserin  |4 aut 
245 1 0 |a Histone deacetylase AtSRT2 regulates salt tolerance during seed germination via repression of vesicle-associated membrane protein 714 (VAMP714) in Arabidopsis 
264 1 |c 2022 
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 20.04.2022 
500 |a Date Revised 10.05.2022 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a © 2022 The Authors. New Phytologist © 2022 New Phytologist Foundation. 
520 |a Salt tolerance during seed germination is essential for seedling establishment under salt stress. Sirtuin-like proteins, NAD+ -dependent histone deacetylases, are involved in plant responses to abiotic stresses; however, the regulatory mechanism remains unknown. We elucidated the mechanism underlying AtSRT2 (a sirtuin-like protein)-mediated regulation of salt tolerance during seed germination in Arabidopsis. The AtSRT2 mutant srt2 exhibited significantly reduced seed germination percentages under salt stress; its targets were identified via chromatin immunoprecipitation coupled with ultra-high-throughput parallel DNA sequencing (ChIP-Seq) assay. Epistasis analysis was performed to identify AtSRT2-related pathways. Overexpression of SRT2.7, an AtSRT2 splice variant, rescued the salt-sensitive phenotype of mutant srt2. AtSRT2 histone deacetylation activity was important for salt tolerance during seed germination. The acetylation level of histone H4K8 locus in srt2-1 increased significantly under salt treatment. Vesicle-associated membrane protein 714 (VAMP714), a negative regulator of hydrogen peroxide (H2 O2 )-containing vesicle trafficking in cells, was identified as a target of AtSRT2. AtSRT2 regulated histone acetylation in the promoter region of VAMP714 and inhibited VAMP714 transcription under salt treatment. Seed germination percentage of double-mutant srt2-1vamp714 was close to that of single-mutant vamp714, and higher than that of single-mutant srt2 under salt stress. Hydrogen peroxide content and DNA damage increased after salt treatment in srt2 during seed germination. AtSRT2 regulates salt tolerance during seed germination through VAMP714 in Arabidopsis 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Arabidopsis 
650 4 |a histone deacetylase 
650 4 |a salt stress 
650 4 |a seed germination 
650 4 |a sirtuin-like protein 
650 4 |a vesicle trafficking 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Histones  |2 NLM 
650 7 |a R-SNARE Proteins  |2 NLM 
650 7 |a Hydrogen Peroxide  |2 NLM 
650 7 |a BBX060AN9V  |2 NLM 
650 7 |a SRT2 protein, Arabidopsis  |2 NLM 
650 7 |a EC 3.5.1.-  |2 NLM 
650 7 |a Sirtuins  |2 NLM 
650 7 |a EC 3.5.1.-  |2 NLM 
650 7 |a Histone Deacetylases  |2 NLM 
650 7 |a EC 3.5.1.98  |2 NLM 
700 1 |a Zhong, Li  |e verfasserin  |4 aut 
700 1 |a Ding, Qing-Qian  |e verfasserin  |4 aut 
700 1 |a Dou, Yi-Ning  |e verfasserin  |4 aut 
700 1 |a Li, Wei-Wei  |e verfasserin  |4 aut 
700 1 |a Xu, Zhao-Shi  |e verfasserin  |4 aut 
700 1 |a Zhou, Yong-Bin  |e verfasserin  |4 aut 
700 1 |a Chen, Jun  |e verfasserin  |4 aut 
700 1 |a Chen, Ming  |e verfasserin  |4 aut 
700 1 |a Ma, You-Zhi  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t The New phytologist  |d 1979  |g 234(2022), 4 vom: 28. Mai, Seite 1278-1293  |w (DE-627)NLM09818248X  |x 1469-8137  |7 nnns 
773 1 8 |g volume:234  |g year:2022  |g number:4  |g day:28  |g month:05  |g pages:1278-1293 
856 4 0 |u http://dx.doi.org/10.1111/nph.18060  |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 234  |j 2022  |e 4  |b 28  |c 05  |h 1278-1293