Type III secretion system effector proteins are mechanically labile

MA LeBlanc, MR Fink, TT Perkins… - Proceedings of the …, 2021 - National Acad Sciences
Multiple gram-negative bacteria encode type III secretion systems (T3SS) that allow them to
inject effector proteins directly into host cells to facilitate colonization. To be secreted …

Oxidation increases the strength of the methionine-aromatic interaction

AK Lewis, KM Dunleavy, TL Senkow, C Her… - Nature chemical …, 2016 - nature.com
Oxidation of methionine disrupts the structure and function of a range of proteins, but little is
understood about the chemistry that underlies these perturbations. Using quantum …

Functional analysis of the interface between the tandem C2 domains of synaptotagmin-1

CS Evans, Z He, H Bai, X Lou, P Jeggle… - Molecular biology of …, 2016 - Am Soc Cell Biol
C2 domains are widespread motifs that often serve as Ca2+-binding modules; some
proteins have more than one copy. An open issue is whether these domains, when …

Structural impact of phosphorylation and dielectric constant variation on synaptotagmin's IDR

ME Fealey, BP Binder, VN Uversky, A Hinderliter… - Biophysical journal, 2018 - cell.com
We used time-resolved Förster resonance energy transfer, circular dichroism, and molecular
dynamics simulation to investigate the structural dependence of synaptotagmin 1's …

Calcium binding promotes conformational flexibility of the neuronal Ca2+ sensor synaptotagmin

M Bykhovskaia - Biophysical Journal, 2015 - cell.com
Abstract Synaptotagmin 1 (Syt1) is a synaptic vesicle protein that serves as a calcium sensor
of neuronal secretion. It is established that calcium binding to Syt1 triggers vesicle fusion …

Synaptotagmin I's intrinsically disordered region interacts with synaptic vesicle lipids and exerts allosteric control over C2A

ME Fealey, R Mahling, AM Rice, K Dunleavy… - Biochemistry, 2016 - ACS Publications
Synaptotagmin I (Syt I) is a vesicle-localized integral membrane protein that senses the
calcium ion (Ca2+) influx to trigger fast synchronous release of neurotransmitter. How the …

Native globular actin has a thermodynamically unstable quasi‐stationary structure with elements of intrinsic disorder

IM Kuznetsova, OI Povarova, VN Uversky… - The FEBS …, 2016 - Wiley Online Library
The native form of globular actin, G‐actin, is formed in vivo as a result of complex post‐
translational folding processes that require ATP energy expenditure and are assisted by the …

The C-terminal domain of the utrophin tandem calponin-homology domain appears to be thermodynamically and kinetically more stable than the full-length protein

S Bandi, SM Singh, KMG Mallela - Biochemistry, 2014 - ACS Publications
Domains are in general less stable than the corresponding full-length proteins. Human
utrophin tandem calponin-homology (CH) domain seems to be an exception. Reversible …

Allostery and instability in the functional plasticity of synaptotagmin I

ME Fealey, A Hinderliter - Communicative & Integrative Biology, 2013 - Taylor & Francis
Synaptotagmin I (Syt I) is the calcium ion sensor for regulated release of neurotransmitter.
How Syt I mediates this cellular event has been a question of extensive study for decades …

Copper binding affinity of the C2B domain of synaptotagmin-1 and its potential role in the nonclassical secretion of acidic fibroblast growth factor

S Jayanthi, KM Kathir, D Rajalingam, M Furr… - … et Biophysica Acta (BBA …, 2014 - Elsevier
Abstract Fibroblast growth factor 1 (FGF1) is a heparin-binding proangiogenic protein. FGF1
lacks the conventional N-terminal signal peptide required for secretion through the …