Determinants of RING-E2 Fidelity for Hrd1p, a Membrane-anchored Ubiquitin Ligase

• Published in: The Journal of biological chemistry Vol. 281; no. 51; pp. 38989 - 39001
• Main Authors: Bazirgan, Omar A., Garza, Renee M., Hampton, Randolph Y.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 22.12.2006; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Motifs; Amino Acid Sequence; Chitin - chemistry; Cytosol - chemistry; Endoplasmic Reticulum - metabolism; Histidine - chemistry; Inteins; Lipid Bilayers - chemistry; Microsomes - metabolism; Molecular Sequence Data; Promoter Regions, Genetic; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - metabolism; Saccharomyces cerevisiae Proteins - physiology; Sequence Homology, Amino Acid; Ubiquitin - chemistry; Ubiquitin-Conjugating Enzymes - metabolism; Ubiquitin-Protein Ligases - chemistry; Ubiquitin-Protein Ligases - physiology

A critical aspect of E3 ubiquitin ligase function is the selection of a particular E2 ubiquitin-conjugating enzyme to accomplish ubiquitination of a substrate. We examined the requirements for correct E2-E3 specificity in the RING-H2 ubiquitin ligase Hrd1p, an ER-localized protein known to use prima...