Browsing by Author "Taylor, JEN"

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    Calmodulin binds a highly extended HIV-1 MA protein that refolds upon its release
    (Cell Press, 2012-08-08) Taylor, JEN; Chow, JYH; Jeffries, CM; Kwan, AH; Duff, AP; Hamilton, WA; Trewhella, J
    Calmodulin (CaM) expression is upregulated upon HIV-1 infection and interacts with proteins involved in viral processing, including the multifunctional HIV-1 MA protein. We present here the results of studies utilizing small-angle neutron scattering with contrast variation that, when considered in the light of earlier fluorescence and NMR data, show CaM binds MA in an extended open-clamp conformation via interactions with two tryptophans that are widely spaced in sequence and space. The interaction requires a disruption of the MA tertiary fold such that MA becomes highly extended in a long snakelike conformation. The CaM-MA interface is extensive, covering ∼70% of the length of the MA such that regions known to be important in MA interactions with critical binding partners would be impacted. The CaM conformation is semiextended and as such is distinct from the classical CaM-collapse about short α-helical targets. NMR data show that upon dissociation of the CaM-MA complex, either by the removal of Ca2+ or increasing ionic strength, MA reforms its native tertiary contacts. Thus, we observe a high level of structural plasticity in MA that may facilitate regulation of its activities via intracellular Ca2+-signaling during viral processing. © 2012 Biophysical Society.
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    (Corrected) Calmodulin binds a highly extended HIV-1 MA protein that refolds upon its release
    (Elsevier, 2023-05-02) Taylor, JEN; Chow, JYH; Jeffries, CM; Kwan, AH; Duff, AP; Hamilton, WA; Trewhella, Jill
    (Biophysical Journal 103, August 2012; 541–549) The authors identified an omission in this article. The figure legend for Figure S2 should include the following: “The model displayed here includes full-length calcium-bound CaM and the matrix protein sequence spanning amino acids 1–113; i.e., it does not include the flexible C-terminal tail (amino acids 114–133).” None of the article's conclusions are affected by this omission. In addition, after publication of the article, the SAXS and SANS data and modeling for this article were deposited in the Small Angle Scattering Biological Data Bank (SASBDB; https://www.sasbdb.org/) under accession code SASDKR3. Finally, the first author's name should appear as “James E. N. Taylor” rather than “James E. Taylor.”