Rapid biophysical characterization and NMR spectroscopy structural analysis of small proteins from bacteria and archaea

  • Proteins encoded by small open reading frames (sORFs) have a widespread occurrence in diverse microorganisms and can be of high functional importance. However, due to annotation biases and their technically challenging direct detection, these small proteins have been overlooked for a long time and were only recently rediscovered. The currently rapidly growing number of such proteins requires efficient methods to investigate their structure–function relationship. Herein, a method is presented for fast determination of the conformational properties of small proteins. Their small size makes them perfectly amenable for solution-state NMR spectroscopy. NMR spectroscopy can provide detailed information about their conformational states (folded, partially folded, and unstructured). In the context of the priority program on small proteins funded by the German research foundation (SPP2002), 27 small proteins from 9 different bacterial and archaeal organisms have been investigated. It is found that most of these small proteins are unstructured or partially folded. Bioinformatics tools predict that some of these unstructured proteins can potentially fold upon complex formation. A protocol for fast NMR spectroscopy structure elucidation is described for the small proteins that adopt a persistently folded structure by implementation of new NMR technologies, including automated resonance assignment and nonuniform sampling in combination with targeted acquisition.
Metadaten
Author:Nina Kubatova, Dennis J. Pyper, Hendrik R. A. Jonker, Krishna SaxenaORCiDGND, Laura Remmel, Christian RichterORCiD, Sabine Brantl, Elena Evguenieva-Hackenberg, Wolfgang Hess, Gabriele Klug, Anita Marchfelder, Jörg SoppaORCiD, Wolfgang Streit, Maxim Mayzel, Vladislav Y. Orekhov, Monika Fuxreiter, Ruth Schmitz-Streit, Harald SchwalbeORCiDGND
URN:urn:nbn:de:hebis:30:3-638192
DOI:https://doi.org/10.1002/cbic.201900677
ISSN:1439-7633
Parent Title (English):ChemBioChem
Publisher:Wiley-VCH
Place of publication:Weinheim
Document Type:Article
Language:English
Date of Publication (online):2019/11/09
Date of first Publication:2019/11/09
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2022/01/25
Tag:NMR spectroscopy; proteomics; small proteins; structural biology; structure–activity relationships
Volume:21
Issue:8
Page Number:10
First Page:1178
Last Page:1187
Note:
This work was supported by the Deutsche Forschungsgemeinschaft (DFG) within the SPP 2002 priority program and the Swedish Research Council (research grant 201504614). Work at BMRZ is supported by the state of Hessen.
HeBIS-PPN:49129400X
Institutes:Biowissenschaften
Wissenschaftliche Zentren und koordinierte Programme / Zentrum für Biomolekulare Magnetische Resonanz (BMRZ)
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften
5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Licence (German):License LogoCreative Commons - Namensnennung 4.0