The shrimp mitochondrial FoF1-ATPase inhibitory factor 1 (IF1)

被引:5
|
作者
Chimeo, Cindy [1 ]
Veronica Fernandez-Gimenez, Analia [2 ]
Campanella, Michelangelo [3 ,4 ]
Mendez-Romero, Ofelia [1 ]
Muhlia-Almazan, Adriana [1 ]
机构
[1] Ctr Invest Alimentac Desarrollo CIAD AC, Bioenerget & Mol Genet Lab, Hermosillo 83000, Sonora, Mexico
[2] Univ Nacl Mar Plata, Fac Ciencias Exactas & Nat, Inst Invest Marinas & Costeras, Lab Fisiol Organismos Acuat, Buenos Aires, DF, Argentina
[3] Univ London, Royal Vet Coll, Dept Comparat Biomed Sci, London, England
[4] UCL, Consortium Mitochondrial Res, London, England
基金
英国生物技术与生命科学研究理事会;
关键词
IF1; FoF1-ATPase; Hypoxia; Inhibitor; Transcriptional regulation; Shrimp; MESSENGER-RNA STABILITY; ATPASE INHIBITOR; LITOPENAEUS-VANNAMEI; REGULATORY PROTEIN; HEART-MITOCHONDRIA; BOVINE F-1-ATPASE; ENCODED SUBUNITS; GENE-EXPRESSION; SWISS-MODEL; SYNTHASE;
D O I
10.1007/s10863-015-9621-0
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The whiteleg shrimp species Litopenaeus vannamei is exposed to cyclic changes of the dissolved oxygen concentration of seawater and must neutralize the adverse effects of hypoxia by using ATP as energy source. In crustaceans, the mitochondrial FOF1-ATP synthase is pivotal to the homeostasis of ATP and function prevalently as a FOF1-ATPase. Hitherto, it is unknown whether these marine invertebrates are equipped with molecules able to control the FOF1-ATPase inhibiting the ATP consumption. In this study, we report two variants of the mitochondrial FOF1-ATPase Inhibitory Factor 1 (IF1) ubiquitously expressed across tissues of the Litopenaeus vannamei transcriptome: the IF1_Lv1 and the IF1_Lv2. The IF1_Lv1, with a full-length sequence of 550 bp, encodes a 104 aa long protein and its mRNA amounts are significantly affected by hypoxia and re-oxygenation. The IF1_Lv2, with a sequence of 654 bp, encodes instead for a protein of 85 aa. Both proteins share a 69 % homology and contain a conserved minimal inhibitory sequence (IATP domain) along with a G-rich region on their N-terminus typical of the invertebrate. In light of this characterization IF1 is here discussed as an adaptive mechanism evolved by this marine species to inhibit the FOF1-ATPase activity and avoid ATP dissipation to thrive in spite of the changes in oxygen tension.
引用
收藏
页码:383 / 393
页数:11
相关论文
共 50 条
  • [31] HYPOXIA-INDUCIBLE FACTOR 1α REGULATES THE EXPRESSION OF THE MITOCHONDRIAL ATPase INHIBITOR PROTEIN (IF1) IN RAT LIVER
    Huang, Li-Ju
    Chuang, I-Chun
    Dong, Huei-Ping
    Yang, Rei-Cheng
    SHOCK, 2011, 36 (01): : 90 - 96
  • [32] Venturicidin-type macrolides as FoF1-ATPase inhibitors: structure-activity relationships
    Tyurin, A.
    Alferova, V.
    Shuvalov, M.
    Novikov, R.
    FEBS OPEN BIO, 2019, 9 : 137 - 137
  • [33] Heart FoF1-ATPase changes during the acute phase of Trypanosoma cruzi infection in rats
    Uyemura, SA
    Jordani, MC
    Polizello, ACM
    Curti, C
    MOLECULAR AND CELLULAR BIOCHEMISTRY, 1996, 165 (02) : 127 - 133
  • [34] The potential role of mitochondrial ATP synthase inhibitory factor 1 (IF1) in coronary heart disease: a literature review
    Maierean, Serban
    Serban, Maria-Corina
    Rizzo, Manfredi
    Lippi, Giuseppe
    Sahebkar, Amirhossein
    Banach, Maciej
    LIPIDS IN HEALTH AND DISEASE, 2017, 16 : 1 - 7
  • [35] Tumor microenvironment responded naturally extracted FOF1-ATPase loaded chromatophores for antitumor therapy
    Hong, Weiyong
    Lou, Bang
    Gao, Ying
    Zhao, Hui
    Ying, Sanjun
    Yang, Saicheng
    Li, Hanbing
    Yang, Qingliang
    Yang, Gensheng
    INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 2023, 230
  • [36] Role of SH-groups in Escherichia coli and Enterococcus hirae FOF1-ATPase functioning
    Poladian, A
    Mnatsakanyan, N
    Bagramyan, K
    Trchounian, A
    FEBS JOURNAL, 2005, 272 : 202 - 202
  • [37] The potential role of mitochondrial ATP synthase inhibitory factor 1 (IF1) in coronary heart disease: a literature review
    Serban Maierean
    Maria-Corina Serban
    Manfredi Rizzo
    Giuseppe Lippi
    Amirhossein Sahebkar
    Maciej Banach
    Lipids in Health and Disease, 16
  • [38] Structure and Flexibility of the C-Ring in the Electromotor of Rotary FoF1-ATPase of Pea Chloroplasts
    Saroussi, Shai
    Schushan, Maya
    Ben-Tal, Nir
    Junge, Wolfgang
    Nelson, Nathan
    PLOS ONE, 2012, 7 (09):
  • [39] The External Stalk of the FoF1-ATPase: 3D-Structure of the b-Dimer
    Volkov, Oleg A.
    Pandey, Susan J.
    Wise, John G.
    Vogel, Pia D.
    BIOPHYSICAL JOURNAL, 2009, 96 (03) : 8A - 8A
  • [40] Insulin-status-dependent modulation of FoF1-ATPase activity in rat liver mitochondria
    Patel, Samir P.
    Katyare, Surendra S.
    LIPIDS, 2006, 41 (07) : 695 - 703