Autotomic behavior of the propeptide in propeptide-mediated folding of prosubtilisin E.

Autotomic behavior of the propeptide in propeptide-mediated folding of prosubtilisin E. Research Abstract Details 

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Autotomic behavior of the propeptide in propeptide-mediated folding of prosubtilisin E. Abstract Text:

Liliana Falzon,Smita Patel,Yu-Jen Chen,Masayori Inouye,

The 77 residue propeptide at the N-terminal end of subtilisin E plays an essential role in subtilisin folding as a tailor-made intramolecular chaperone. Upon completion of folding, the propeptide is autoprocessed and removed by subtilisin digestion. This propeptide-mediated protein folding has been used as a paradigm for the study of protein folding. Here, we show by three independent methods, that the propeptide domain and the subtilisin domain show distinctive intrinsic stability that is obligatory for efficient autoprocessing of the propeptide domain. Two tryptophan residues, Trp106 and Trp113, on the surface of subtilisin located on one of the two helices that form the interface between the propeptide and the subtilisin domains play a key role in maintaining the distinctive instability of the propeptide domain, after completion of folding. When either of the Trp residues was substituted with Tyr, the characteristic biphasic heat denaturation profile of two domains unfolding was not observed, resulting in a single transition of denaturation. The results provide evidence that the propeptide not only plays an essential role in subtilisin folding, but upon completion of folding it behaves as an independent domain. Once the propeptide-mediated folding is completed, the propeptide domain is readily eliminated without interference from the subtilisin domain. This "autotomic" behavior of the propeptide may be a prevailing principle in propeptide-mediated protein folding.

Autotomic behavior of the propeptide in propeptide-mediated folding of prosubtilisin E. Publishing Authors By Initials

L Falzon,S Patel,YJ Chen,M Inouye,

For similar enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: trypsin research abstracts see: enzymes and coenzymes: enzymes: hydrolases: peptide hydrolases: endopeptidases: serine endopeptidases: trypsin research

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Autotomic behavior of the propeptide in propeptide-mediated folding of prosubtilisin E. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Journal of molecular biology

VOLUME: 366

Page Numbers: 494-503

Journal Abbreviation: J. Mol. Biol.

ISSN: 0022-2836

DAY: 10

MONTH: 11

YEAR: 2006

Autotomic behavior of the propeptide in propeptide-mediated folding of prosubtilisin E. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985088

Autotomic behavior of the propeptide in propeptide-mediated folding of prosubtilisin E. Keywords Mesh Terms:

KEYWORDS: Trypsin

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Autotomic behavior of the propeptide in propeptide-mediated folding of prosubtilisin E. Information

Substance Name: Trypsin

Registry Number: EC 3.4.21.4

Grant and Affiliation Information for Autotomic behavior of the propeptide in propeptide-mediated folding of prosubtilisin E.

AFFILIATION: Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, NJ 08854, USA.

Country: England

AGENCY: United States NIGMS

GRANT: GM51966

ACRONYM: GM

MEDLINETA: J Mol Biol

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