E. Krysztofinska

MdfA is a novel ClpC adaptor protein that functions in the developing Bacillus subtilis spore

Shawn C. Massoni, Nicola J. Evans, Ingo Hantke, Colleen Fenton et autres

Bacterial protein degradation machinery consists of chaperone–protease complexes that play vital roles in bacterial growth and development and have sparked interest as novel antimicrobial targets. ClpC–ClpP (ClpCP) is one such chaperone–protease complex, recruited by adaptors to specific functions in the model bacterium …

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MdfA is a novel ClpC adaptor protein that functions in the developing Bacillus subtilis spore

Shawn C. Massoni, Nicola J. Evans, Ingo Hantke, Colleen Fenton et autres

ABSTRACT Bacterial protein degradation machinery consists of chaperone-protease complexes that play vital roles in bacterial growth and development and have sparked interest as novel antimicrobial targets. ClpC-ClpP (ClpCP) is one such chaperone-protease, recruited by adaptors to specific functions in the model bacterium …

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Mapping of a N-terminal α-helix domain required for human PINK1 stabilization, Serine228 autophosphorylation and activation in cells

Poonam S. Kakade, Hina Ojha, Olawale G. Raimi, Andrew M. Shaw et autres

gene are causal for Parkinson's disease (PD). PINK1 encodes a mitochondrial localized protein kinase that is a master-regulator of mitochondrial quality control pathways. Structural studies to date have elaborated the mechanism of how mutations located within the kinase domain disrupt PINK1 function; …

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Mapping of a N-terminal α-helix domain required for human PINK1 stabilisation, Serine228 autophosphorylation and activation in cells

Poonam S. Kakade, Hina Ojha, Olawale G. Raimi, Andrew M. Shaw et autres

Abstract Human autosomal recessive mutations in the PINK1 gene are causal for Parkinson’s disease (PD). PINK1 encodes a mitochondrial localised protein kinase that is a master-regulator of mitochondrial quality control pathways. Structural studies to date have elaborated the mechanism of how mutations …

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Genetic, structural, and functional analysis of pathogenic variations causing methylmalonyl-CoA epimerase deficiency

Kathrin Heuberger, H. Bailey, Patricie Burda, A. Chaikuad et autres

Human methylmalonyl-CoA epimerase (MCEE) catalyzes the interconversion of d-methylmalonyl-CoA and l-methylmalonyl-CoA in propionate catabolism. Autosomal recessive pathogenic variations in MCEE reportedly cause methylmalonic aciduria (MMAuria) in eleven patients. We investigated a cohort of 150 individuals suffering from MMAuria of unknown origin, identifying …

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Genetic, structural, and functional analysis of mutations causing methylmalonyl-CoA epimerase deficiency

Kathrin Heuberger, H. Bailey, Patricie Burda, A. Chaikuad et autres

Abstract Human methylmalonyl-CoA epimerase ( MCEE ) catalyzes the interconversion of D-methylmalonyl-CoA and L-methylmalonyl-CoA in propionate catabolism. Autosomal recessive mutations in MCEE reportedly cause methylmalonic aciduria (MMAuria) in eleven patients. We investigated a cohort of 150 individuals suffering from MMAuria of unknown …

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Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control

Santiago Martínez‐Lumbreras, E. Krysztofinska, Arjun Thapaliya, Alessandro Spilotros et autres

BACKGROUND: Protein quality control mechanisms are essential for cell health and involve delivery of proteins to specific cellular compartments for recycling or degradation. In particular, stray hydrophobic proteins are captured in the aqueous cytosol by a co-chaperone, the small glutamine-rich, tetratricopeptide repeat-containing …

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Structural and Functional Insights into Bacillus subtilis Sigma Factor Inhibitor, CsfB

Santiago Martínez‐Lumbreras, Caterina Alfano, Nicola J. Evans, Katherine M. Collins et autres

Global changes in bacterial gene expression can be orchestrated by the coordinated activation/deactivation of alternative sigma (σ) factor subunits of RNA polymerase. Sigma factors themselves are regulated in myriad ways, including via anti-sigma factors. Here, we have determined the solution structure of …

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The roles of the co-chaperone SGTA/Sgt2, the BAG6 complex and E3 ubiquitin ligase RNF126 in cytosolic quality control

E. Krysztofinska

Backbone assignment of SGTA N-terminal domain including linker residues

Santiago Martinez Lumbreras, E. Krysztofinska, Rivka Leah Isaacson

Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp

E. Krysztofinska, Nicola J. Evans, Arjun Thapaliya, James W. Murray et autres

Small glutamine-rich tetratricopeptide repeat-containing protein 2 (Sgt2) is a multi-module co-chaperone involved in several protein quality control pathways. The TPR domain of Sgt2 and several other proteins, including SGTA, Hop, and CHIP, is a highly conserved motif known to form transient complexes …

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A novel RNA polymerase‐binding protein that interacts with a sigma‐factor docking site

Anna F. Wang-Erickson, Padraig Deighan, Shanshan Chen, Kelsey Barrasso et autres

Summary Sporulation in Bacillus subtilis is governed by a cascade of alternative RNA polymerase sigma factors. We previously identified a small protein Fin that is produced under the control of the sporulation sigma factor σF to create a negative feedback loop that …

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