ATP-Citrate Lyase Is Required for Production of Cytosolic Acetyl Coenzyme A and Development in Aspergillus nidulans

被引:73
|
作者
Hynes, Michael J. [1 ]
Murray, Sandra L. [1 ]
机构
[1] Univ Melbourne, Dept Genet, Parkville, Vic 3010, Australia
基金
澳大利亚研究理事会;
关键词
FUNGUS SORDARIA-MACROSPORA; CARBON SOURCE UTILIZATION; ACETATE REGULATORY GENE; SACCHAROMYCES-CEREVISIAE; A SYNTHETASE; FUNCTIONAL-ANALYSIS; CARNITINE ACETYLTRANSFERASE; TRANSCRIPTIONAL ACTIVATOR; PYRUVATE DECARBOXYLASE; HISTONE ACETYLATION;
D O I
10.1128/EC.00080-10
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Acetyl coenzyme A (CoA) is a central metabolite in carbon and energy metabolism and in the biosynthesis of cellular molecules. A source of cytoplasmic acetyl-CoA is essential for the production of fatty acids and sterols and for protein acetylation, including histone acetylation in the nucleus. In Saccharomyces cerevisiae and Candida albicans acetyl-CoA is produced from acetate by cytoplasmic acetyl-CoA synthetase, while in plants and animals acetyl-CoA is derived from citrate via ATP-citrate lyase. In the filamentous ascomycete Aspergillus nidulans, tandem divergently transcribed genes (aclA and aclB) encode the subunits of ATP-citrate lyase, and we have deleted these genes. Growth is greatly diminished on carbon sources that do not result in cytoplasmic acetyl-CoA, such as glucose and proline, while growth is not affected on carbon sources that result in the production of cytoplasmic acetyl-CoA, such as acetate and ethanol. Addition of acetate restores growth on glucose or proline, and this is dependent on facA, which encodes cytoplasmic acetyl-CoA synthetase, but not on the regulatory gene facB. Transcription of aclA and aclB is repressed by growth on acetate or ethanol. Loss of ATP-citrate lyase results in severe developmental effects, with the production of asexual spores (conidia) being greatly reduced and a complete absence of sexual development. This is in contrast to Sordaria macrospora, in which fruiting body formation is initiated but maturation is defective in an ATP-citrate lyase mutant. Addition of acetate does not repair these defects, indicating a specific requirement for high levels of cytoplasmic acetyl-CoA during differentiation. Complementation in heterokaryons between aclA and aclB deletions for all phenotypes indicates that the tandem gene arrangement is not essential.
引用
收藏
页码:1039 / 1048
页数:10
相关论文
共 50 条
  • [41] GENETIC TARGET VALIDATION FOR ATP-CITRATE LYASE INHIBITION
    Ference, Brian A.
    Neff, David
    Cabot, Martin
    Catapano, Alberico
    Ray, Kausik
    [J]. JOURNAL OF THE AMERICAN COLLEGE OF CARDIOLOGY, 2017, 69 (11) : 1655 - 1655
  • [42] A RADIOCHEMICAL ASSAY FOR ATP-CITRATE LYASE IN NERVOUS TISSUES
    SMITH, JC
    DEERY, A
    DADAMO, AF
    [J]. BRAIN RESEARCH, 1970, 23 (03) : 443 - &
  • [43] ATP-citrate lyase is essential for macrophage inflammatory response
    Infantino, Vittoria
    Iacobazzi, Vito
    Palmieri, Ferdinando
    Menga, Alessio
    [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2013, 440 (01) : 105 - 111
  • [44] EFFECT OF OXALOACETATE AND PHOSPHORYLATION ON ATP-CITRATE LYASE ACTIVITY
    PENTYALA, SN
    BENJAMIN, WB
    [J]. BIOCHEMISTRY, 1995, 34 (35) : 10961 - 10969
  • [45] DEPENDENCE OF ATP-CITRATE LYASE KINASE-ACTIVITY ON THE PHOSPHORYLATION OF ATP-CITRATE LYASE BY CYCLIC AMP-DEPENDENT PROTEIN-KINASE
    RAMAKRISHNA, S
    PUCCI, DL
    BENJAMIN, WB
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1983, 258 (08) : 4950 - 4956
  • [46] ATP citrate lyase mediated cytosolic acetyl-CoA biosynthesis increases mevalonate production in Saccharomyces cerevisiae
    Sarah Rodriguez
    Charles M. Denby
    T. Van Vu
    Edward E. K. Baidoo
    George Wang
    Jay D. Keasling
    [J]. Microbial Cell Factories, 15
  • [47] ATP citrate lyase mediated cytosolic acetyl-CoA biosynthesis increases mevalonate production in Saccharomyces cerevisiae
    Rodriguez, Sarah
    Denby, Charles M.
    Van Vu, T.
    Baidoo, Edward E. K.
    Wang, George
    Keasling, Jay D.
    [J]. MICROBIAL CELL FACTORIES, 2016, 15
  • [48] An allosteric mechanism for potent inhibition of human ATP-citrate lyase
    Wei, Jia
    Leit, Silvana
    Kuai, Jun
    Therrien, Eric
    Rafi, Salma
    Harwood, H. James, Jr.
    DeLaBarre, Byron
    Tong, Liang
    [J]. NATURE, 2019, 568 (7753) : 566 - +
  • [49] The multifaceted therapeutic value of targeting ATP-citrate lyase in atherosclerosis
    Verberk, Sanne G. S.
    Kuiper, Kirsten L.
    Lauterbach, Mario A.
    Latz, Eicke
    Van den Bossche, Jan
    [J]. TRENDS IN MOLECULAR MEDICINE, 2021, 27 (12) : 1095 - 1105
  • [50] ATP-citrate lyase regulates lipid biosynthesis in Yarrowia lipolytica
    Anche, Varsha Chowdary
    Fakas, Stylianos
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2023, 299 (03) : S437 - S437