Orthopoxvirus protein F1 / Poxvirus F1/C10 / Apoptosis regulator M11L like / host cell mitochondrial outer membrane / Bcl-2-like superfamily / regulation of apoptotic process / membrane / Apoptosis regulator OPG045
Function and homology information
Biological species
Vaccinia virus
Citation
Journal: J Biol Chem / Year: 2016 Title: The N Terminus of the Vaccinia Virus Protein F1L Is an Intrinsically Unstructured Region That Is Not Involved in Apoptosis Regulation. Authors: Sofia Caria / Bevan Marshall / Robyn-Lee Burton / Stephanie Campbell / Delara Pantaki-Eimany / Christine J Hawkins / Michele Barry / Marc Kvansakul / Abstract: Subversion of host cell apoptotic responses is a prominent feature of viral immune evasion strategies to prevent premature clearance of infected cells. Numerous poxviruses encode structural and ...Subversion of host cell apoptotic responses is a prominent feature of viral immune evasion strategies to prevent premature clearance of infected cells. Numerous poxviruses encode structural and functional homologs of the Bcl-2 family of proteins, and vaccinia virus harbors antiapoptotic F1L that potently inhibits the mitochondrial apoptotic checkpoint. Recently F1L has been assigned a caspase-9 inhibitory function attributed to an N-terminal α helical region of F1L spanning residues 1-15 (1) preceding the domain-swapped Bcl-2-like domains. Using a reconstituted caspase inhibition assay in yeast we found that unlike AcP35, a well characterized caspase-9 inhibitor from the insect virus Autographa californica multiple nucleopolyhedrovirus, F1L does not prevent caspase-9-mediated yeast cell death. Furthermore, we found that deletion of the F1L N-terminal region does not impede F1L antiapoptotic activity in the context of a viral infection. Solution analysis of the F1L N-terminal regions using small angle x-ray scattering indicates that the region of F1L spanning residues 1-50 located N-terminally from the Bcl-2 fold is an intrinsically unstructured region. We conclude that the N terminus of F1L is not involved in apoptosis inhibition and may act as a regulatory element in other signaling pathways in a manner reminiscent of other unstructured regulatory elements commonly found in mammalian prosurvival Bcl-2 members including Bcl-xL and Mcl-1.
Instrument name: Australian Synchrotron SAXS/WAXS / City: Melbourne / 国: Australia / Shape: Point / Type of source: X-ray synchrotron / Dist. spec. to detc.: 1.6 mm
Detector
Name: Pilatus 1M
Scan
Title: Vaccinia MVA F1L antiapoptotic Bcl-2 protein / Measurement date: Apr 15, 2016 / Storage temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 18 / Unit: 1/nm /
Min
Max
Q
0.196
5.1598
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 335 /
Min
Max
Q
0.196003
2.34086
P(R) point
1
335
R
0
16.2
Result
D max: 16.2 / Type of curve: single_conc /
Experimental
Porod
MW
51.7 kDa
-
Volume
-
74.36 nm3
Guinier
P(R)
Forward scattering, I0
0.0735086
-
Radius of gyration, Rg
3.41 nm
3.68 nm
+
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