Work

Role of methionine-1 in ubiquitin conformation and activity

Year: 1986

Type: article

Abstract: Methionine-1 of ubiquitin was oxidized to the sulfone without significant effect on biological activity or conformation at neutral pH. However, at low pH, the oxidized protein expanded to a more open conformation, similar in gel sieving properties to denatured ubiquitin but similar in secondary structure to native ubiquitin. This conformational transition was absent in the native protein. Interpretation of these results in the light of X-ray data suggests that ubiquitin contains two independently folded domains that are held together in part by a hydrogen bond between Met-1 and Lys-63 and which can be separated when this bond is broken. It is suggested that separation of these domains may occur upon ubiquitin conjugation.

Source: Biochemical and Biophysical Research Communications

DOI: 10.1016/0006-291x(86)90300-1

Authors: Esther Breslow, Yeshpal Chauhan, Reynold Daniel, Suresh Tate

Institution: Cornell University

Language: English

Topic: Ubiquitin and proteasome pathways

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,110

Funder: National Institute of General Medical Sciences