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January 25, 2019

Volume 294Issue 4p1083-1436
Open Access
On The Cover: The figure shows the structure of the F1-c8 subcomplex of mitochondrial ATP synthase (PDB ID: 2XND). The rotor ring is composed of eight c-subunits (green and red), with Lys-43 (indicated in cyan on red c-subunit) being ubiquitously trimethylated in all Metazoa. Małecki et al., pages 1128–1141, identify FAM173B as the long-sought mitochondrial methyltransferase responsible for trimethylation of Lys-43 in the c-subunit and show that this modification improves ATP synthase function....
On The Cover: The figure shows the structure of the F1-c8 subcomplex of mitochondrial ATP synthase (PDB ID: 2XND). The rotor ring is composed of eight c-subunits (green and red), with Lys-43 (indicated in cyan on red c-subunit) being ubiquitously trimethylated in all Metazoa. Małecki et al., pages 1128–1141, identify FAM173B as the long-sought mitochondrial methyltransferase responsible for trimethylation of Lys-43 in the c-subunit and show that this modification improves ATP synthase function.

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Bioenergetics

Cell Biology

Enzymology

Gene Regulation

Glycobiology and Extracellular Matrices

Immunology

Lipids

Membrane Biology

Methods and Resources

Molecular Biophysics

Plant Biology

Protein Structure and Folding

Protein Synthesis and Degradation

Signal Transduction

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