Tertiary structural rearrangements upon oxidation of Methionine145 in calmodulin promotes targeted proteasomal degradation

The selectivity underlying the recognition of oxidized calmodulin (CaM) by the 20S proteasome in complex with Hsp90 was identified using mass spectrometry. We find that degradation of oxidized CaM (CaMox) occurs in a multistep process, which involves an initial cleavage that releases a large N-termi...

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Veröffentlicht in:	Biophysical Journal, 91(4):1480-1493 91(4):1480-1493, 2006-08, Vol.91 (4), p.1480-1493
Hauptverfasser:	Sacksteder, Colette A, Whittier, Jennifer E, Xiong, Yijia, Li, Jinhui, Galeva, Nadezhda A, Jacoby, Michael E, Purvine, Samuel O, Williams, Todd D, Rechsteiner, Martin C, Bigelow, Diana J, Squier, Thomas C
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Animals BASIC BIOLOGICAL SCIENCES calcium sensors CALMODULIN Calmodulin - chemistry Cattle CLEAVAGE DIGESTION Environmental Molecular Sciences Laboratory HSP90 Heat-Shock Proteins - chemistry HYDROGEN PEROXIDE Kinetics MASS SPECTROSCOPY METABOLISM METHIONINE Methionine - chemistry MORPHOLOGICAL CHANGES MUTAGENESIS MUTANTS OXIDATION Oxidation-Reduction oxidative stress PEPTIDES Proteasome Endopeptidase Complex - analysis Proteasome Endopeptidase Complex - chemistry protein degradation Protein Denaturation Protein Structure, Tertiary Proteins Radioisotopes - chemistry signal transduction SPECIFICITY Structure-Activity Relationship SULFOXIDES
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