دورية أكاديمية

Amino acid substitutions around the chromophore of the chromoprotein Rtms5 influence polypeptide cleavage

التفاصيل البيبلوغرافية
العنوان: Amino acid substitutions around the chromophore of the chromoprotein Rtms5 influence polypeptide cleavage
المؤلفون: Turcic, Kristina, Pettikiriarachchi, Anne, Battad, Jion, Wilmann, Pascal G., Rossjohn, Jamie, Dove, Sophie G., Devenish, Rodney J., Prescott, Mark
المساهمون: W. Baumeister
بيانات النشر: Academic Press Inc Elsevier Science
سنة النشر: 2006
المجموعة: The University of Queensland: UQ eSpace
مصطلحات موضوعية: Biochemistry & Molecular Biology, Biophysics, All-protein Chromophores, Rtms5, Chromoprotein, Structure, Acylimine Bond, Red Fluorescent Protein, Gfp-like Proteins, Crystal-structure, Anemonia-sulcata, Resolution, Coral, 270199 Biochemistry and Cell Biology not elsewhere classified, C1, 780105 Biological sciences
الوصف: Extension of the conjugated pi-system of many all-protein chromophores with an acylimine bond is the basis for their red-shifted optical properties. The presence of this post-translational modification is evident in crystal structures of these proteins. Harsh denaturation of proteins containing an acylimine bond results in partial polypeptide cleavage. For the red fluorescent protein DsRed, the extent of cleavage is quantitative. However, this is not the case for the blue non-fluorescent chromoprotein Rtms5, even though all chromophores in tetrameric Rtms5 contain an acylimine bond. We have identified two positions around the chromophore of Rtms5 where substitutions can promote or suppress the extent of cleavage on harsh denaturation. We propose a model in which cleavage of Rtms5 is facilitated by a trans to cis isomerisation of the chromophore. (c) 2006 Elsevier Inc. All rights reserved.
نوع الوثيقة: article in journal/newspaper
اللغة: English
تدمد: 0006-291X
العلاقة: orcid:0000-0003-1823-8634
الإتاحة: https://doi.org/10.1016/j.bbrc.2005.12.118Test
https://espace.library.uq.edu.au/view/UQ:79522Test
رقم الانضمام: edsbas.266C706A
قاعدة البيانات: BASE