Histone acetyltransferase MoHat1 acetylates autophagy-related proteins MoAtg3 and MoAtg9 to orchestrate functional appressorium formation and pathogenicity in Magnaporthe oryzae. Issue 7 (3rd July 2019)
- Record Type:
- Journal Article
- Title:
- Histone acetyltransferase MoHat1 acetylates autophagy-related proteins MoAtg3 and MoAtg9 to orchestrate functional appressorium formation and pathogenicity in Magnaporthe oryzae. Issue 7 (3rd July 2019)
- Main Title:
- Histone acetyltransferase MoHat1 acetylates autophagy-related proteins MoAtg3 and MoAtg9 to orchestrate functional appressorium formation and pathogenicity in Magnaporthe oryzae
- Authors:
- Yin, Ziyi
Chen, Chen
Yang, Jie
Feng, Wanzhen
Liu, Xinyu
Zuo, Rongfang
Wang, Jingzhen
Yang, Lina
Zhong, Kaili
Gao, Chuyun
Zhang, Haifeng
Zheng, Xiaobo
Wang, Ping
Zhang, Zhengguang - Abstract:
- ABSTRACT: Macroautophagy/autophagy is critical for normal appressorium formation and pathogenicity of the rice blast fungus Magnaporthe oryzae, but the molecular base of autophagy linked to pathogenicity remains elusive in this or other pathogenic fungi. We found that MoHat1, a histone acetyltransferase (HAT) homolog, had a role in the regulation of autophagy through the acetylation of autophagy related proteins MoAtg3 and MoAtg9. We also found that MoHat1 was subject to regulation by the protein kinase MoGsk1 that modulated the translocation of MoHat1 from the nucleus to the cytoplasm with the assistance of MoSsb1, a protein chaperone. The alternation of intracellular location affected MoHat1 in the modification of cytosolic autophagy proteins that maintained normal autophagy. Furthermore, we provided evidence linking acetylation of MoAtg3 and MoAtg9 by MoHat1 to functional appressorium development and pathogenicity. Together with the first report of MoAtg9 being subject to acetylation regulation by MoHat1, our studies depicted how MoHat1 regulated autophagy in conjunction with MoGsk1 and how normal autophagy was linked to appressorium formation and function and pathogenicity of M. oryzae . Abbreviations : A/Ala: alanine; AP: autophagosome; Atg genes/proteins: autophagy-related genes/proteins; BiFC: bimolecular fluorescence complementation; co-IP: co-immunoprecipitation; DAPI: 4ʹ, 6-diamidino-2-phenylindole; D/Asp: aspartic acid; GFP: green fluorescent protein; GSK3:ABSTRACT: Macroautophagy/autophagy is critical for normal appressorium formation and pathogenicity of the rice blast fungus Magnaporthe oryzae, but the molecular base of autophagy linked to pathogenicity remains elusive in this or other pathogenic fungi. We found that MoHat1, a histone acetyltransferase (HAT) homolog, had a role in the regulation of autophagy through the acetylation of autophagy related proteins MoAtg3 and MoAtg9. We also found that MoHat1 was subject to regulation by the protein kinase MoGsk1 that modulated the translocation of MoHat1 from the nucleus to the cytoplasm with the assistance of MoSsb1, a protein chaperone. The alternation of intracellular location affected MoHat1 in the modification of cytosolic autophagy proteins that maintained normal autophagy. Furthermore, we provided evidence linking acetylation of MoAtg3 and MoAtg9 by MoHat1 to functional appressorium development and pathogenicity. Together with the first report of MoAtg9 being subject to acetylation regulation by MoHat1, our studies depicted how MoHat1 regulated autophagy in conjunction with MoGsk1 and how normal autophagy was linked to appressorium formation and function and pathogenicity of M. oryzae . Abbreviations : A/Ala: alanine; AP: autophagosome; Atg genes/proteins: autophagy-related genes/proteins; BiFC: bimolecular fluorescence complementation; co-IP: co-immunoprecipitation; DAPI: 4ʹ, 6-diamidino-2-phenylindole; D/Asp: aspartic acid; GFP: green fluorescent protein; GSK3: glycogen synthase kinase 3; HAT: histone acetyltransferase; Hsp70: heat-shock protein 70; IH: invasive hyphae; K/Lys: lysine; MMS: methyl methanesulfonate; Mo: Magnaporthe oryzae ; PAS: phagophore assembly site; PE: phosphatidylethanolamine; PtdIns3K: phosphatidylinositol 3-kinase; R/Arg: arginine; S/Ser: serine; T/Thr: threonine; TOR: target of rapamycin; WT: wild type; YFP: yellow fluorescent protein … (more)
- Is Part Of:
- Autophagy. Volume 15:Issue 7(2019)
- Journal:
- Autophagy
- Issue:
- Volume 15:Issue 7(2019)
- Issue Display:
- Volume 15, Issue 7 (2019)
- Year:
- 2019
- Volume:
- 15
- Issue:
- 7
- Issue Sort Value:
- 2019-0015-0007-0000
- Page Start:
- 1234
- Page End:
- 1257
- Publication Date:
- 2019-07-03
- Subjects:
- Acetylation -- appressorium -- autophagy -- histone acetyltransferase -- Magnaporthe oryzae -- pathogenicity
Autophagic vacuoles -- Periodicals
Apoptosis -- Periodicals
Cell death -- Periodicals
Lysosomes -- Periodicals
Degeneration (Pathology) -- Periodicals
Autophagy -- Periodicals
Cell Death -- Periodicals
Lysosomes -- Periodicals
Periodicals
571.936 - Journal URLs:
- http://www.tandfonline.com/loi/kaup20#.Vd3NN_lVhBc ↗
http://www.landesbioscience.com/journals/autophagy ↗
http://www.tandfonline.com/ ↗ - DOI:
- 10.1080/15548627.2019.1580104 ↗
- Languages:
- English
- ISSNs:
- 1554-8627
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 1835.065800
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 10832.xml