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Full-Text Articles in Life Sciences
Binding Of The Molecular Chaperone Alphab-Crystallin To Abeta Amyloid Fibrils Inhibits Fibril Elongation, Sarah L. Shammas, Christopher A. Waudby, Shuyu Wang, Alexander K. Buell, Tuomas P. Knowles, Heath W. Ecroyd, Mark E. Welland, John A. Carver, Christopher M. Dobson, Sarah Meehan
Binding Of The Molecular Chaperone Alphab-Crystallin To Abeta Amyloid Fibrils Inhibits Fibril Elongation, Sarah L. Shammas, Christopher A. Waudby, Shuyu Wang, Alexander K. Buell, Tuomas P. Knowles, Heath W. Ecroyd, Mark E. Welland, John A. Carver, Christopher M. Dobson, Sarah Meehan
Heath Ecroyd
The molecular chaperone αB-crystallin is a small heat-shock protein that is upregulated in response to a multitude of stress stimuli, and is found colocalized with Aβ amyloid fibrils in the extracellular plaques that are characteristic of Alzheimer's disease. We investigated whether this archetypical small heat-shock protein has the ability to interact with Aβ fibrils in vitro. We find that αB-crystallin binds to wild-type Aβ42 fibrils with micromolar affinity, and also binds to fibrils formed from the E22G Arctic mutation of Aβ42. Immunoelectron microscopy confirms that binding occurs along the entire length and ends of the fibrils. Investigations into the effect …
Subunit Exchange Of Polydisperse Proteins: Mass Spectrometry Reveals Consequences Of Αa-Crystallin Truncation, J. Andrew Aquilina, Justin Benesch, Lin Lin Ding, Orna Yaron, Joseph Horwitz, Carol Robinson
Subunit Exchange Of Polydisperse Proteins: Mass Spectrometry Reveals Consequences Of Αa-Crystallin Truncation, J. Andrew Aquilina, Justin Benesch, Lin Lin Ding, Orna Yaron, Joseph Horwitz, Carol Robinson
J. A. Aquilina
The small heat shock protein, α-crystallin, plays a key role in maintaining lens transparency by chaperoning structurally compromised proteins. This is of particular importance in the human lens, where proteins are exposed to post-translational modifications over the life-time of an individual. Here, we examine the structural and functional consequences of one particular modification of αA-crystallin involving the truncation of 5 C-terminal residues (αA1–168). Using novel mass spectrometry approaches and established biophysical techniques, we show that αA1–168 forms oligomeric assemblies with a lower average molecular mass than wild-type αA-crystallin (αAWT). Also apparent from the mass spectra of both αAWT and αA1–168 …
3-Hydroxykynurenine Oxidizes Alpha-Crystallin: Potential Role In Cataractogenesis, Roger Truscott, Andrew Aquilina, Peter Hains, Anastasia Korlimbinis
3-Hydroxykynurenine Oxidizes Alpha-Crystallin: Potential Role In Cataractogenesis, Roger Truscott, Andrew Aquilina, Peter Hains, Anastasia Korlimbinis
J. A. Aquilina
No abstract provided.
The Small Heat-Shock Proteins Hspb2 And Hspb3 Form Well-Defined Heterooligomers In A Unique 3 To 1 Subunit Ratio, J. Den Engelsman, S. Baros, P. Y. W. Dankers, B. Kamps, W. T. Vree Egberts, C. S. Bode, L. A. Lane, J. A. Aquilina, J. L. P. Benesch, C. V. Robinson, W. W. De Jong, W. C. Boelens
The Small Heat-Shock Proteins Hspb2 And Hspb3 Form Well-Defined Heterooligomers In A Unique 3 To 1 Subunit Ratio, J. Den Engelsman, S. Baros, P. Y. W. Dankers, B. Kamps, W. T. Vree Egberts, C. S. Bode, L. A. Lane, J. A. Aquilina, J. L. P. Benesch, C. V. Robinson, W. W. De Jong, W. C. Boelens
J. A. Aquilina
Various mammalian small heat-shock proteins (sHSPs) can interact with one another to form large polydisperse assemblies. In muscle cells, HSPB2/MKBP (myotonic dystrophy protein kinase-binding protein) and HSPB3 have been shown to form an independent complex. To date, the biochemical properties of this complex have not been thoroughly characterized. In this study, we show that recombinant HSPB2 and HSPB3 can be successfully purified from E.coli cells co-expressing both proteins. Nanoelectrospray ionization mass spectrometry and sedimentation velocity analytical ultracentrifugation analysis showed that HSPB2/B3 forms a series of well defined hetero-oligomers, consisting of 4, 8, 12, 16, 20 and 24 subunits, each maintaining …
Evidence For Specific Subunit Distribution And Interactions In The Quaternary Structure Of Α-Crystallin, Amie M. Morris, J Andrew Aquilina
Evidence For Specific Subunit Distribution And Interactions In The Quaternary Structure Of Α-Crystallin, Amie M. Morris, J Andrew Aquilina
J. A. Aquilina
The quaternary structure of alpha-crystallin is dynamic, a property which has thwarted crystallographic efforts towards structural characterization. In this study, we have used collision-induced dissociation mass spectrometry to examine the architecture of the polydisperse assemblies of alpha-crystallin. For total alpha-crystallin isolated directly from fetal calf lens using size-based chromatography, the alpha B-crystallin subunit was found to be preferentially dissociated from the oligomers, despite being significantly less abundant overall than the alpha A-crystallin subunits. Furthermore, upon mixing molar equivalents of purified alpha A- and alpha B-crystallin, the levels of their dissociation were found to decrease and increase, respectively, with time. Interestingly …
Mimicking Phosphorylation Of Alphab-Crystallin Affects Its Chaperone Activity, Heath W. Ecroyd, Sarah Meehan, J Horwitz, Andrew Aquilina, J L Benesch, C V Robinson, Cait Macphee, John Carver
Mimicking Phosphorylation Of Alphab-Crystallin Affects Its Chaperone Activity, Heath W. Ecroyd, Sarah Meehan, J Horwitz, Andrew Aquilina, J L Benesch, C V Robinson, Cait Macphee, John Carver
J. A. Aquilina
No abstract provided.