NDLI: Analysis of the structure and stability of omega loop A replacements in yeast iso-1-cytochrome c.

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Analysis of the structure and stability of omega loop A replacements in yeast iso-1-cytochrome c.

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Analysis of the structure and stability of omega loop A replacements in yeast iso-1-cytochrome c.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Fetrow, J. S. Oehrl, W. Horner, S. R. Boose, T. L. Schaak, D. L. Burton, R. E.
Description	Country affiliation: United States Author Affiliation: Fetrow JS ( Department of Biological Sciences, University at Albany, SUNY 12222, USA. jacque@isadora.albany.edu)
Abstract	Omega (omega)-loop A, residues 18-32 in wild-type yeast iso-1-cytochrome c, has been deleted and replaced with loop sequences from three other cytochromes c and one from esterase. Yeast expressing a partial loop deletion do not contain perceptible amounts of holoprotein as measured by low-temperature spectroscopy and cannot grow on nonfermentable media. Strains expressing loop replacement mutations accumulate holoprotein in vivo, but the protein function varies depending on the sequence and length of the replacement loop; in vivo expression levels do not correlate with their thermal denaturation temperatures. In vitro spectroscopic studies of the loop replacement proteins indicate that all fold into a native-like cytochrome c conformation, but are less stable than the wild-type protein. Decreases in thermal stability are caused by perturbation of loop C backbone in one case and a slight reorganization of the protein hydrophobic core in another case, rather than rearrangement of the loop A backbone. A single-site mutation in one of the replacement mutants designed to relieve inefficient hydrophobic core packing caused by the new loop recovers some, but not all, of the lost stability.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	1
Volume Number	6
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1997-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cytochrome c Group Chemistry Cytochromes c Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Enzymology Amino Acid Sequence Circular Dichroism Enzyme Stability Hot Temperature Molecular Sequence Data Protein Conformation Growth & Development Spectrophotometry, Ultraviolet Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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