Document Detail


Local Unfolding Is Required for the Site-Specific Protein Modification by Transglutaminase.
MedLine Citation:
PMID:  23083324     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The transglutaminase (TGase) from Streptomyces mobaraensis catalyzes transamidation reactions in a protein substrate leading to the modification of the side chains of Gln and Lys residues according to the A-CONH(2) + H(2)N-B → A-CONH-B + NH(3) reaction, where both A and B can be a protein or a ligand. A noteworthy property of TGase is its susbstrate specificity, so that often only a few specific Gln or Lys residues can be modified in a globular protein. The molecular features of a globular protein dictating the site-specific reactions mediated by TGase are yet poorly understood. Here, we have analyzed the reactivity toward TGase of apomyoglobin (apoMb), α-lactalbumin (α-LA), and fragment 205-316 of thermolysin. These proteins are models of protein structure and folding that have been studied previously using the limited proteolysis technique to unravel regions of local unfolding in their amino acid sequences. The three proteins were modified by TGase at the level of Gln or Lys residues with dansylcadaverine or carbobenzoxy-l-glutaminylglycine, respectively. Despite these model proteins containing several Gln and Lys residues, the sites of TGase derivatization occur over restricted chain regions of the protein substrates. In particular, the TGase-mediated modifications occur in the "helix F" region in apoMb, in the β-domain in apo-α-LA in its molten globule state, and in the N-terminal region in fragment 205-316 of thermolysin. Interestingly, the sites of limited proteolysis are located in the same chain regions of these proteins, thus providing a clear-cut demonstration that chain flexibility or local unfolding overwhelmingly dictates the site-specific modification by both TGase and a protease.
Authors:
Barbara Spolaore; Samanta Raboni; Amparo Ramos Molina; Abhijeet Satwekar; Nunzio Damiano; Angelo Fontana
Related Documents :
6161984 - Changes in rna and protein synthesis in the neural retina during lens regeneration in n...
23546624 - Refolding of sds-denatured proteins using amphipathic cosolvents and osmolytes.
3975654 - Progestin modulation of estrogen-dependent marker protein synthesis in the endometrium.
7508744 - Protein synthesis in splanchnic tissues of sheep offered two levels of intake.
1639184 - Concepts in protein folding.
3881624 - Ultrastructural evidence for the synthesis of serum amyloid a protein by murine hepatoc...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-10-19
Journal Detail:
Title:  Biochemistry     Volume:  -     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-22     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
CRIBI Biotechnology Centre, University of Padua , Viale G. Colombo 3, 35121 Padua, Italy.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Differential expression of parvalbumin interneurons in neonatal phencyclidine treated rats and socia...
Next Document:  Rhythmic neuronal activity in S2 somatosensory and insular cortices contribute to the initiation of ...