We also generated some mutants in which combinations of different sites are mutated.
Fluorescence-activated cell sorting identified mutants in which lipid accumulation is increased.
We prepared phage libraries expressing LIGHT mutants in which all the lysine residues were replaced with other amino acids.
Analysis of mutants in which the phosphorylated amino acids were replaced by alanine, either individually or in various combinations, identified S174 as the functional phosphorylation site.
These difficulties generate a limitation for studying the functions of TuMV mutants, in which weaker infectivity may be incurred by mutations.
(a) mutants lacking an intrinsic salt bridge, (b) mutants lacking a common salt bridge, (c) mutants in which a salt bridge may have been introduced.
We mutated each amino acid individually to alanine, and we also generated mutants in which various combinations of phosphorylation sites were changed to alanine.
(a, b) mutants lacking an intrinsic salt bridge, (c, d) mutants lacking a common salt bridge, (e, f) mutants in which a salt bridge may have been introduced.
In addition, the phenotypes of 147 mutants, in which these genes have been disrupted or knocked down, have been summarized and discussed.
The mutants in which loops 1 and/or 3 were replaced also showed decreased activity, but they still maintained some activities.
We have constructed and characterised mutants in which this pocket is filled by large hydrophobic side-chains replacing alanine at position 82.
