scholarly journals Human COQ10A and COQ10B are distinct lipid-binding START domain proteins required for coenzyme Q function

2019 ◽  
Vol 60 (7) ◽  
pp. 1293-1310 ◽  
Author(s):  
Hui S. Tsui ◽  
Nguyen V. B. Pham ◽  
Brendan R. Amer ◽  
Michelle C. Bradley ◽  
Jason E. Gosschalk ◽  
...  
Keyword(s):  
Coenzyme Q ◽  
Lipid Binding ◽  
Start Domain ◽  
Q Function

scholarly journals StAR-Related Lipid Transfer (START) Domains Across the Rice Pangenome Reveal How Ontogeny Recapitulated Selection Pressures During Rice Domestication

2021 ◽  
Vol 12 ◽  
Author(s):  
Sanjeet Kumar Mahtha ◽  
Ravi Kiran Purama ◽  
Gitanjali Yadav
Keyword(s):  
Lipid Binding ◽  
Chromosomal Mapping ◽  
Specific Substrate ◽  
Limited Information ◽  
Lipid Transfer ◽  
Rice Varieties ◽  
Selection Pressures ◽  
Preferential Expression ◽  
Start Domain ◽  
Rice Domestication

The StAR-related lipid transfer (START) domain containing proteins or START proteins, encoded by a plant amplified family of evolutionary conserved genes, play important roles in lipid binding, transport, signaling, and modulation of transcriptional activity in the plant kingdom, but there is limited information on their evolution, duplication, and associated sub- or neo-functionalization. Here we perform a comprehensive investigation of this family across the rice pangenome, using 10 wild and cultivated varieties. Conservation of START domains across all 10 rice genomes suggests low dispensability and critical functional roles for this family, further supported by chromosomal mapping, duplication and domain structure patterns. Analysis of synteny highlights a preponderance of segmental and dispersed duplication among STARTs, while transcriptomic investigation of the main cultivated variety Oryza sativa var. japonica reveals sub-functionalization amongst genes family members in terms of preferential expression across various developmental stages and anatomical parts, such as flowering. Ka/Ks ratios confirmed strong negative/purifying selection on START family evolution, implying that ontogeny recapitulated selection pressures during rice domestication. Our findings provide evidence for high conservation of START genes across rice varieties in numbers, as well as in their stringent regulation of Ka/Ks ratio, and showed strong functional dependency of plants on START proteins for their growth and reproductive development. We believe that our findings advance the limited knowledge about plant START domain diversity and evolution, and pave the way for more detailed assessment of individual structural classes of START proteins among plants and their domain specific substrate preferences, to complement existing studies in animals and yeast.

scholarly journals The START domain Coq10 polypeptide binds Coenzyme Q and is required for mitochondrial respiratory electron transport

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Susan Morvaridi ◽  
Ryoichi Saiki ◽  
Wei‐Siang Liau ◽  
Tadashi Kawashima ◽  
Cathy Clarke
Keyword(s):  
Electron Transport ◽  
Coenzyme Q ◽  
Start Domain ◽  
Respiratory Electron Transport ◽  
Mitochondrial Respiratory

scholarly journals Structure and functionality of a multimeric human COQ7:COQ9 complex

2021 ◽  
Author(s):  
Mateusz Manicki ◽  
Halil Aydin ◽  
Luciano A. Abriata ◽  
Katherine A. Overmyer ◽  
Rachel M. Guerra ◽  
...  
Keyword(s):  
Antioxidant Defense ◽  
Binding Capacity ◽  
Coenzyme Q ◽  
Lipid Binding ◽  
Mitochondrial Inner Membrane ◽  
Access Channel ◽  
Redox Active ◽  
Oligomeric Complex ◽  
Dynamics Simulations ◽  
Functional Analyses

Coenzyme Q (CoQ, ubiquinone) is a redox-active lipid essential for core metabolic pathways and antioxidant defense. CoQ is synthesized upon the mitochondrial inner membrane by an ill-defined 'complex Q' metabolon. Here we present a structure and functional analyses of a substrate- and NADH-bound oligomeric complex comprised of two complex Q subunits: the hydroxylase COQ7, which performs the penultimate step in CoQ biosynthesis, and the prenyl lipid-binding protein COQ9. We reveal that COQ7 adopts a modified ferritin-like fold with an extended hydrophobic access channel whose substrate binding capacity is enhanced by COQ9. Using molecular dynamics simulations, we further show that two COQ7:COQ9 heterodimers form a curved tetramer that deforms the membrane, potentially opening a pathway for CoQ intermediates to translocate from within the bilayer to the proteins' lipid-binding sites. Two such tetramers assemble into a soluble octamer, closed like a capsid, with lipids captured within. Together, these observations indicate that COQ7 and COQ9 cooperate to access hydrophobic precursors and coordinate subsequent synthesis steps toward producing mature CoQ.

Modes of coenzyme Q function in electron transfer

PROTOPLASMA ◽  
1995 ◽  
Vol 184 (1-4) ◽  
pp. 50-62 ◽  
Author(s):  
G. Lenaz ◽  
Carla Bovina ◽  
Cinzia Castelluccio ◽  
Marika Cavazzoni ◽  
E. Estornell ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Coenzyme Q ◽  
Q Function

scholarly journals An Isoprene Lipid-Binding Protein Promotes Eukaryotic Coenzyme Q Biosynthesis

2019 ◽  
Vol 73 (4) ◽  
pp. 763-774.e10 ◽  
Author(s):  
Danielle C. Lohman ◽  
Deniz Aydin ◽  
Helaina C. Von Bank ◽  
Robert W. Smith ◽  
Vanessa Linke ◽  
...  
Keyword(s):  
Binding Protein ◽  
Coenzyme Q ◽  
Lipid Binding ◽  
Lipid Binding Protein

Coenzyme Q Function in Mitochondria

2020 ◽  
pp. 51-89
Author(s):  
Maria Luisa Genova ◽  
Giorgio Lenaz
Keyword(s):  
Coenzyme Q ◽  
Q Function

scholarly journals Arabidopsis PROTODERMAL FACTOR2 binds lysophosphatidylcholines and transcriptionally regulates phospholipid metabolism

2021 ◽  
Author(s):  
Izabela Wojciechowska ◽  
Thiya Mukherjee ◽  
Patrick Knox-Brown ◽  
Xueyun Hu ◽  
Aashima Khosla ◽  
...  
Keyword(s):  
Target Genes ◽  
Affinity Purification ◽  
Regulatory Protein ◽  
Lipid Binding ◽  
Epidermal Differentiation ◽  
In Vitro Assays ◽  
Dependent Manner ◽  
Lipid Transfer ◽  
Start Domain

Plant homeodomain leucine-zipper IV (HD-Zip IV) transcription factors (TFs) contain an evolutionarily conserved steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domain. The START domain is required for TF activity; however, its presumed role as a lipid sensor is not well understood. Here we used tandem affinity purification from Arabidopsis cell cultures to demonstrate that PROTODERMAL FACTOR2 (PDF2), a representative family member which controls epidermal differentiation, recruits lysophosphatidylcholines in a START-dependent manner. In vitro assays with recombinant protein verified that a missense mutation in a predicted ligand contact site reduces lysophospholipid binding. We additionally uncovered that PDF2 controls the expression of phospholipid-related target genes by binding to a palindromic octamer with consensus to a phosphate (Pi) response element. Phospholipid homeostasis and elongation growth were altered in pdf2 mutants according to Pi availability. Cycloheximide chase experiments further revealed a role for START in maintaining protein levels, and Pi limitation resulted in enhanced protein destabilization, suggesting a mechanism by which lipid binding controls TF activity. We propose that the START domain serves as a molecular sensor for membrane phospholipid status in the epidermis. Overall our data provide insights towards understanding how the lipid metabolome integrates Pi availability with gene expression.

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