Biophysical Studies of LC3 Family Proteins

2019 ◽  
pp. 91-117
Author(s):  
Javier H. Hervás ◽  
Zuriñe Antón ◽  
Alicia Alonso
Keyword(s):  
Biophysical Studies

scholarly journals Insight into the HIV-1 Vif SOCS-box–ElonginBC interaction

Open Biology ◽  
2013 ◽  
Vol 3 (11) ◽  
pp. 130100 ◽  
Author(s):  
Zhisheng Lu ◽  
Julien R. C. Bergeron ◽  
R. Andrew Atkinson ◽  
Torsten Schaller ◽  
Dennis A. Veselkov ◽  
...  
Keyword(s):  
Solution Structure ◽  
Hydrophobic Interactions ◽  
Dynamic Information ◽  
Ubiquitin Ligase Complex ◽  
Biophysical Studies ◽  
Viral Infectivity Factor ◽  
Β Sheet ◽  
Socs Box ◽  
Insight Into ◽  
Hiv 1

The HIV-1 viral infectivity factor (Vif) neutralizes cell-encoded antiviral APOBEC3 proteins by recruiting a cellular ElonginB (EloB)/ElonginC (EloC)/Cullin5-containing ubiquitin ligase complex, resulting in APOBEC3 ubiquitination and proteolysis. The suppressors-of-cytokine-signalling-like domain (SOCS-box) of HIV-1 Vif is essential for E3 ligase engagement, and contains a BC box as well as an unusual proline-rich motif. Here, we report the NMR solution structure of the Vif SOCS–ElonginBC (EloBC) complex. In contrast to SOCS-boxes described in other proteins, the HIV-1 Vif SOCS-box contains only one α-helical domain followed by a β-sheet fold. The SOCS-box of Vif binds primarily to EloC by hydrophobic interactions. The functionally essential proline-rich motif mediates a direct but weak interaction with residues 101–104 of EloB, inducing a conformational change from an unstructured state to a structured state. The structure of the complex and biophysical studies provide detailed insight into the function of Vif's proline-rich motif and reveal novel dynamic information on the Vif–EloBC interaction.

scholarly journals BIOPHYSICAL STUDIES OF BLOOD PLASMA PROTEINS

1946 ◽  
Vol 165 (1) ◽  
pp. 21-35 ◽  
Author(s):  
H.F. Deutsch ◽  
R.A. Alberty ◽  
L.J. Gosting
Keyword(s):  
Blood Plasma ◽  
Plasma Proteins ◽  
Biophysical Studies ◽  
Blood Plasma Proteins

scholarly journals Biophysical studies of cholesterol effects on chromatin

2017 ◽  
Vol 58 (5) ◽  
pp. 934-940 ◽  
Author(s):  
Isabel T. G. Silva ◽  
Vinícius Fernandes ◽  
Caio Souza ◽  
Werner Treptow ◽  
Guilherme M. Santos
Keyword(s):  
Biophysical Studies

Biochemical and biophysical studies of the interaction of class I antiarrhythmic drugs with the cardiac sodium channel

1994 ◽  
Vol 33 (3) ◽  
pp. 277-294 ◽  
Author(s):  
Gerald W. Zamponi ◽  
Henry J. Duff ◽  
Robert J. French ◽  
Robert S. Sheldon
Keyword(s):  
Sodium Channel ◽  
Antiarrhythmic Drugs ◽  
Class I ◽  
Cardiac Sodium Channel ◽  
Biophysical Studies

Biophysical Studies of the Immunoglobulins

1971 ◽  
Vol 40 (4-5) ◽  
pp. 551-575 ◽  
Author(s):  
G.W. Litman ◽  
A. Rosenberg ◽  
D. Frommel ◽  
B. Pollara ◽  
J. Finstad ◽  
...  
Keyword(s):  
Biophysical Studies

Biophysical studies of the interaction between calmodulin and the R287-T311 region of human estrogen receptor α reveals an atypical binding process

2012 ◽  
Vol 419 (2) ◽  
pp. 356-361 ◽  
Author(s):  
Ludovic Carlier ◽  
Cillian Byrne ◽  
Emeric Miclet ◽  
Sandrine Bourgoin-Voillard ◽  
Magali Nicaise ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Binding Process ◽  
Biophysical Studies ◽  
Human Estrogen Receptor

Biophysical Studies of Cells from the Carotid Body of the Rabbit

1990 ◽  
pp. 31-43
Author(s):  
M. R. Duchen ◽  
T. J. Biscoe ◽  
M. Valdeolmillos
Keyword(s):  
Carotid Body ◽  
Biophysical Studies

scholarly journals Fission yeast myosin Myo2 is down-regulated in actin affinity by light chain phosphorylation

2017 ◽  
Vol 114 (35) ◽  
pp. E7236-E7244 ◽  
Author(s):  
Luther W. Pollard ◽  
Carol S. Bookwalter ◽  
Qing Tang ◽  
Elena B. Krementsova ◽  
Kathleen M. Trybus ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Light Chain ◽  
Force Production ◽  
Class Ii ◽  
Cell System ◽  
Cell Cortex ◽  
Animal Cells ◽  
Contractile Ring ◽  
Biophysical Studies

Studies in fission yeast Schizosaccharomyces pombe have provided the basis for the most advanced models of the dynamics of the cytokinetic contractile ring. Myo2, a class-II myosin, is the major source of tension in the contractile ring, but how Myo2 is anchored and regulated to produce force is poorly understood. To enable more detailed biochemical/biophysical studies, Myo2 was expressed in the baculovirus/Sf9 insect cell system with its two native light chains, Rlc1 and Cdc4. Milligram yields of soluble, unphosphorylated Myo2 were obtained that exhibited high actin-activated ATPase activity and in vitro actin filament motility. The fission yeast specific chaperone Rng3 was thus not required for expression or activity. In contrast to nonmuscle myosins from animal cells that require phosphorylation of the regulatory light chain for activation, phosphorylation of Rlc1 markedly reduced the affinity of Myo2 for actin. Another unusual feature of Myo2 was that, unlike class-II myosins, which generally form bipolar filamentous structures, Myo2 showed no inclination to self-assemble at approximately physiological salt concentrations, as analyzed by sedimentation velocity ultracentrifugation. This lack of assembly supports the hypothesis that clusters of Myo2 depend on interactions at the cell cortex in structural units called nodes for force production during cytokinesis.

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