Misincorporation of the proline homologue Aze (azetidine-2-carboxylic acid) into recombinant myelin basic protein.

Amino Acid Substitution; Animals; Azetidinecarboxylic Acid/chemistry/metabolism/pharmacology; Escherichia coli/drug effects/growth & development/metabolism; Mice; Molecular Structure; Myelin Basic Protein/chemistry/metabolism; Polymers; Proline/analogs & derivatives/chemistry/metabolism; Protein Conformation; Recombinant Proteins/chemistry/metabolism

Abstract :

[en] We have evaluated the effects of the proline homologue Aze (1) (azetidine-2-carboxylic acid) on growth of Escherichia coli strains used to over-express recombinant forms of murine myelin basic protein (rmMBP), and on the degree of misincorporation. Addition of Aze to minimal media resulted in severe diminution of growth rate, but rmMBP could still be produced and purified. Mass spectrometry indicated that a detectable proportion of the rmMBP produced had incorporated Aze instead of proline (Pro), to a maximum of three of eleven possible sites. Molecular modelling of a proline-rich region of rmMBP illustrated that the misincorporation of Aze at any site would cause a severe bend in the polypeptide chain, and that multiple Pro-->Aze substitutions would completely disrupt a poly-proline type II structure that has been conjectured to be functionally significant.

Disciplines :

Biochemistry, biophysics & molecular biology

Author, co-author :

Bessonov, Kyrylo ; Université de Liège - ULiège > Dép. d'électric., électron. et informat. (Inst.Montefiore) > Bioinformatique

Bamm, Vladimir V.

Harauz, George

Language :

English

Title :

Misincorporation of the proline homologue Aze (azetidine-2-carboxylic acid) into recombinant myelin basic protein.

Publication date :

2010

Journal title :

Phytochemistry

ISSN :

0031-9422

eISSN :

1873-3700

Publisher :

Elsevier, Netherlands

Volume :

Issue :

5-6

Pages :

502-7

Peer reviewed :

Peer Reviewed verified by ORBi

Commentary :

Available on ORBi :

since 06 March 2013

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