Intrinsic disorder in the common N-terminus of human adenovirus 5 E1B-55K and its related E1BN proteins indicated by studies on E1B-93R

Sieber, Timo and Scholz, Roland and Spoerner, Michael and Schumann, Frank and Kalbitzer, Hans Robert and Dobner, Thomas (2011) Intrinsic disorder in the common N-terminus of human adenovirus 5 E1B-55K and its related E1BN proteins indicated by studies on E1B-93R. VIROLOGY, 418 (2). pp. 133-143. ISSN 0042-6822,

Full text not available from this repository. (Request a copy)

Abstract

The El B transcription unit of human adenovirus encodes at least five different proteins generated by alternative splicing of a common El B precursor mRNA. E1B-156R, -93R and -84R contain individual carboxy termini but share a common amino terminus. To acquire data on the structure of the amino terminus we performed biophysical analyses on E1B-93R. We show that E1B-93R is mostly unstructured and fulfills the criteria of an intrinsically disordered protein (IDP). The intrinsic disorder in the amino terminus of these proteins is evolutionary conserved in all seven human adenovirus species. As IDPs comprise a rapidly growing family of proteins which, despite their lack of a well defined structure, often fulfill essential regulatory functions, the observations described here might open up a new avenue for the understanding of the regulation and functions of E1B proteins, in particular the multifunctional E1B-55K oncoprotein. (c) 2011 Elsevier Inc. All rights reserved.

Item Type: Article
Uncontrolled Keywords: AMINO-ACID-RESIDUES; BRILLIANT BLUE R-250; EARLY REGION 1B; POLYACRYLAMIDE GEL-ELECTROPHORESIS; SECONDARY STRUCTURE PREDICTION; NATIVELY UNFOLDED PROTEINS; HUMAN-PAROTID SALIVA; DNA-BINDING; UNSTRUCTURED PROTEINS; PROLINE-RICH; Adenovirus; E1B-55K; Intrinsically disordered proteins (IDPs)
Subjects: 500 Science > 570 Life sciences
Divisions: Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Depositing User: Dr. Gernot Deinzer
Date Deposited: 29 May 2020 10:40
Last Modified: 29 May 2020 10:40
URI: https://pred.uni-regensburg.de/id/eprint/20153

Actions (login required)

View Item View Item