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Publikováno v:
The Journal of Biological Chemistry
The bacterial type VI secretion system (T6SS) delivers effectors into eukaryotic host cells or toxins into bacterial competitor for survival and fitness. The T6SS is positively regulated by the threonine phosphorylation pathway (TPP) and negatively b
Autor:
Kelli L. Hvorecny, Kyle C. Cady, Jennifer M. Bomberger, Alicia E. Ballok, Andrew A. Bridges, Christopher D. Bahl, George A. O'Toole, Dean R. Madden
Publikováno v:
Journal of Biological Chemistry. 289:7460-7469
Endocytic recycling of the cystic fibrosis transmembrane conductance regulator (CFTR) is blocked by the CFTR inhibitory factor (Cif). Originally discovered in Pseudomonas aeruginosa, Cif is a secreted epoxide hydrolase that is transcriptionally regul
Autor:
Mitsuhiro Ueda, Shoko Shinya, Taro Tamada, Kazutaka Miyatake, Masami Nakazawa, Noriko Kawamoto, Tamo Fukamizo, Takao Arimori, Nobuo Okazaki
Publikováno v:
Journal of Biological Chemistry. 288:18696-18706
Chitinase C from Ralstonia sp. A-471 (Ra-ChiC) has a catalytic domain sequence similar to goose-type (G-type) lysozymes and, unlike other chitinases, belongs to glycohydrolase (GH) family 23. Using NMR spectroscopy, however, Ra-ChiC was found to inte
Publikováno v:
Journal of Biological Chemistry. 288:8479-8490
Several gram-positive pathogenic bacteria employ near-iron transporter (NEAT) domains to acquire heme from hemoglobin during infection. However, the structural requirements and mechanism of action for NEAT-mediated heme extraction remains unknown. Ba
Autor:
Francisca A. Cerda-Maira, Huib Ovaa, Stevan R. Hubbard, Julian Mintseris, Kristin E. Burns, K. Heran Darwin, Fiona E. McAllister, Steven P. Gygi, Elke E. Noens, Francesco D. Melandri, Matthias Wilmanns, Carsten Schwerdtfeger
Publikováno v:
Journal of Biological Chemistry. 287:37522-37529
Deamidase of Pup (Dop), the prokaryotic ubiquitin-like protein (Pup)-deconjugating enzyme, is critical for the full virulence of Mycobacterium tuberculosis and is unique to bacteria, providing an ideal target for the development of selective chemothe
Autor:
Yoshinori Fujiyoshi, Tomoya Imai, Katsumasa Irie, Kazuya Kitagawa, Hitoshi Nagura, Takushi Shimomura
Publikováno v:
Journal of Biological Chemistry. 285:3685-3694
Prokaryotic voltage-gated sodium channels (Na(V)s) are homotetramers and are thought to inactivate through a single mechanism, named C-type inactivation. Here we report the voltage dependence and inactivation rate of the NaChBac channel from Bacillus
Autor:
Anthony Ludlam, Joseph S. Brunzelle, Thomas Pribyl, Sharon H. Ackerman, Xingjue Xu, Domenico L. Gatti
Publikováno v:
The Journal of Biological Chemistry
Mitochondrial F(1)-ATPase contains a hexamer of alternating alpha and beta subunits. The assembly of this structure requires two specialized chaperones, Atp11p and Atp12p, that bind transiently to beta and alpha. In the absence of Atp11p and Atp12p,
Autor:
Hiroki Ashida, Antoine Danchin, Agnieszka Sekowska, Tomoko Sakiyama, Nicole Tandeau de Marsac, Yohtaro Saito, Akiho Yokota
Publikováno v:
Journal of Biological Chemistry. 284:13256-13264
The sequences classified as genes for various ribulose-1,5-bisphosphate (RuBP) carboxylase/oxygenase (RuBisCO)-like proteins (RLPs) are widely distributed among bacteria, archaea, and eukaryota. In the phylogenic tree constructed with these sequences
Publikováno v:
Journal of Biological Chemistry. 283:2846-2857
The cytochrome bc(1) complex (bc(1)) is a major contributor to the proton motive force across the membrane by coupling electron transfer to proton translocation. The crystal structures of wild type and mutant bc(1) complexes from the photosynthetic p
Publikováno v:
JOURNAL OF BIOLOGICAL CHEMISTRY. 281(15):10533-10539
Signal peptide peptidases (SPPs) are enzymes involved in the initial degradation of signal peptides after they are released from the precursor proteins by signal peptidases. In contrast to the eukaryotic enzymes that are aspartate peptidases, the cat