Structural characterization of Tobacco etch virus coat protein mutants.
Structural characterization of Tobacco etch virus coat protein mutants.
复制标题
烟草蚀纹病毒外壳蛋白突变体的结构表征。
DOI：
10.1007/s00705-003-0247-x
复制
发表时间：
2004
影响因子：
2.7
通讯作者：
Beachy,RN
中科院分区：
文献类型：
--
作者：
Voloudakis,AE;Malpica,CA;Aleman-Verdaguer,M-E;Stark,DM;Fauquet,CM;Beachy,RN
The assembly of Tobacco etch potyvirus (TEV) coat protein (CP) and truncated mutants inEscherichia coliwas studied. CP from which 28, 63 or 112 amino acids were deleted from the N-terminus polymerized into potyvirus-like particles (PVLPs). These structures were more rigid and progressively smaller in diameter than those produced by full length TEV-CP. CP from which 175 N-terminal amino acids were removed, failed to polymerize. A fragment containing amino acids 131 to 206 of TEV-CP is sufficient for PVLP assembly inE. coli.To determine the function of the highly conserved amino acids Ser152, Arg154, and Asp198 point mutants were generated. The mutant CPΔ63(Asp198Glu) exhibited different spectral properties following circular dichroism analysis showing a lower amount of α-helix compared to the wild type molecule. No differences were observed in spectra obtained from fluorescence spectroscopy. The point mutants bind RNAin vitroto the same degree as the wild type protein. However, while the wild type and the Arg154Gln mutant CP were each able to form PVLPs inE. coli, the Asp198Glu and the double mutant Ser152Pro/Arg154Gln mutants did not. These results suggest that the Asp198Glu mutation has an altered secondary structure which affects the capacity of the protein to polymerize but did not affectin vitroprotein-RNA interactions.
影响因子：
3
作者：
John E. Johnson;J. Speir
通讯作者：
J. Speir