Arthur E. Johnson, PhD
Regents Professor Emeritus
Department of Molecular &
Education & Professional Appointments
Johnson received a BS in chemistry from the California Institute of Technology in 1964. After teaching and coaching football at Milton Academy near Boston for five years, he earned his PhD in chemistry at the University of Oregon in 1973. Following postdoctoral research at Columbia University on a Helen Hay Whitney Fellowship, he joined the faculty of the Department of Chemistry and Biochemistry at the University of Oklahoma in 1977, where he was named the Grayce B. Kerr Centennial Chair in 1992 before moving to Texas A&M in 1994. Johnson was named a Texas A&M Regents Professor in 2004 and a Distinguished Professor of Molecular & Cellular Medicine in 2008. He held the Wehner-Welch Foundation Chair in the College of Medicine at the Texas A&M University Health Science Center from 1994 to 2013. He was also a Distinguished Professor of Chemistry and a Professor of Biochemistry and Biophysics at Texas A&M. Johnson has taught lecture and laboratory courses in biochemistry, biophysics, chemistry, and physics at various levels.
The Johnson lab investigated several biochemical processes, including the movement of proteins through or into a membrane (protein trafficking), nascent protein folding, ER-associated degradation (ERAD) of misfolded proteins, and the creation of holes in mammalian cell membranes by bacterial toxins. Two other processes that were examined extensively are blood coagulation and protein biosynthesis. The molecular machinery involved in each of these complex processes consists largely of multi-component complexes of proteins or of proteins and nucleic acids, most of which are membrane-bound. Research and published work therefore includes studies of protein-membrane, protein-nucleic acid, protein-protein, and protein-metal ion interactions.
To examine how these processes are accomplished and regulated at the molecular level, the lab employed a variety of biophysical, biochemical, and other techniques. Multiple fluorescence techniques were used to detect and characterize, both kinetically and thermodynamically, the molecular interactions and conformational changes involved in the assembly, function, and regulation of free and membrane-bound macromolecular complexes, as well as to determine their structure and topography. Also used were fluorescence resonance energy transfer (FRET), photocrosslinking, and chemical crosslinking to detect nascent protein folding, to determine the spatial arrangement of individual components within the complexes, to identify which components or residues are adjacent to each other, and to quantify the magnitude of conformational changes in the complexes. Importantly, all the biophysical experiments examined functional molecules in fully assembled multi-component complexes in/on intact membranes in aqueous solution so they could directly correlate structure and function.
- Lin, P.-J., Jongsma, C. G., Liao, S., and Johnson, A. E. (2011) "Transmembrane Segments of Nascent Polytopic Membrane Proteins Control Cytosol/ER Targeting during Membrane Integration ," Journal of Cell Biology 195, 41-54.
- Lin, P.-J., Jongsma, C. G., Pool, M. R., and Johnson, A. E. (2011) "Polytopic Membrane Protein Folding at L17 in the Ribosome Tunnel Initiates Cyclical Changes at the Translocon," Journal of Cell Biology 195, 55-70.
- Khushoo, A., Yang, Z., Johnson, A. E., and Skach, W. R. (2011) "Ligand-Driven Vectorial Folding of Ribosome-Bound Human CFTR NBD1," Molecular Cell 41, 682-692.
- Devaraneni, P., Conti, B., Matsumura, Y., Yang, Z., Johnson, A. E., and Skach, W. R. (2011) “Stepwise Insertion and Inversion of a Type II Signal Anchor Occurs in the Ribosome-Sec61 Complex,” Cell 146, 134-147.
- Hotze, E. M., Wilson-Kubalek, E., Farrand, A. J., Bentsen, L., Parker, M. W., Johnson, A. E., and Tweten, R. K. (2012) "Monomer-Monomer Interactions Propagate Structural Transitions Necessary for Pore Formation by the Cholesterol-Dependent Cytolysins," Journal of Biological Chemistry 287, 24534-24543.
- Hou, B., Lin, P.-J., and Johnson, A. E. (2012) "Membrane Protein TM Segments Are Retained at the Translocon during Integration Until the Nascent Chain Cues FRET-Detected Release into the Lipid Phase," Molecular Cell 48, 398-408.
- Sato, T. K., Tweten, R. K., and Johnson, A. E.* (2013) "Disulfide-Bond Scanning Reveals Assembly State and b-Strand Tilt Angle of the PFO b-Barrel," Nature Chemical Biology 9, 383-389.
- Malhotra, K., Sathappa, M., Landin, J. S., Johnson, A. E., and Alder, N. N. (2013) "Structural Changes in the Mitochondrial Tim23 Channel Are Coupled to the Protonmotive Force," Nature Structural and Molecular Biology 20, 965-972.
- Karamyshev, A. L., Patrick, A. E., Karamysheva, Z. N., Griesemer, D. S., Hudson, H., Tjon-Kon-Sang, S., Nilsson, I., Otto, H., Liu, Q., Rospert, S., von Heijne, G., Johnson, A. E., and Thomas, P. J. (2014) "Inefficient SRP Interaction with a Nascent Chain Triggers a mRNA Quality Control Pathway," Cell 156, 146-157.
- Mayerhofer PU, Bañó-Polo M, Mingarro I, Johnson AE. (2016) “Human Peroxin PEX3 Is Co-translationally Integrated into the ER and Exits the ER in Budding Vesicles.” Traffic 17, 117-30.