title: Oligomerization state of photosynthetic core complexes is correlated with the dimerization affinity of a transmembrane helix.
abstract: In the Rhodobacter (Rba.) species of photosynthetic purple bacteria, a single transmembrane α-helix, PufX, is found within the core complex, an essential photosynthetic macromolecular assembly that performs the absorption and the initial processing of light energy. Despite its structural simplicity, many unresolved questions surround PufX, the most important of which is its location within the photosynthetic core complex. One proposed placement of PufX is at the center of a core complex dimer, where two PufX helices associate in the membrane and form a homodimer. Inability for PufX of certain Rba. species to form a homodimer is thought to lead to monomeric core complexes. In the present study, we employ a combination of computational and experimental techniques to test the hypothesized homodimerization of PufX. We carry out a systematic investigation to measure the dimerization affinity of PufX from four Rba. species, Rba. blasticus , Rba. capsulatus , Rba. sphaeroides , and Rba. veldkampii , using a molecular dynamics-based free-energy method, as well as experimental TOXCAT assays. We found that the four PufX helices have substantially different dimerization affinities. Both computational and experimental techniques demonstrate that species with dimeric core complexes have PufX that can potentially form a homodimer, whereas the one species with monomeric core complexes has a PufX with little to no dimerization propensity. Our analysis of the helix-helix interface revealed a number of positions that may be important for PufX dimerization and the formation of a hydrogen-bond network between these GxxxG-containing helices. Our results suggest that the different oligomerization states of core complexes in various Rba. species can be attributed, among other factors, to the different propensity of its PufX helix to homodimerize.
authors.affiliation: Department of Physics and Beckman Institute for Advanced Science and Engineering, University of Illinois at Urbana-Champaign, 61801, United States.
authors.forename: Jen
authors.initials: J
authors.lastname: Hsin
authors.forename: Loren M
authors.initials: LM
authors.lastname: LaPointe
authors.forename: Alla
authors.initials: A
authors.lastname: Kazy
authors.forename: Christophe
authors.initials: C
authors.lastname: Chipot
authors.forename: Alessandro
authors.initials: A
authors.lastname: Senes
authors.forename: Klaus
authors.initials: K
authors.lastname: Schulten
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D016992:Rhodobacter / Q000737:chemistry*; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes; C088749:PufX protein, Rhodobacter