Colombo, Noemi and Schroeder, Josef and Cabrele, Chiara (2006) A short Id2 protein fragment containing the nuclear export signal forms amyloid-like fibrils. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 346 (1). pp. 182-187. ISSN 0006-291X, 1090-2104
Full text not available from this repository. (Request a copy)Abstract
The negative regulator of DNA-binding/cell-differentiation Id2 is a small protein containing a central helix-loop-helix (HLH) motif and a C-terminal nuclear export signal (NES). Whereas the former is essential for Id2 dimerization and nuclear localization, the latter is responsible for the transport of Id2 from the nucleus to the cytoplasm. Whereas the isolated Id2 HLH motif is highly helical, large C-terminal Id2 fragments including the NES sequence are either unordered or aggregation-prone. To study the conformational properties of the isolated NES region, we synthesized the Id2 segment 103-124. The latter was insoluble in water and only temporarily soluble in water/alcohol mixtures, where it formed quickly precipitating beta-sheets. Introduction of a positively charged N-terminal tail prevented aggressive precipitation and led to aggregates consisting of long fibrils that bound thioflavin T. These results show an interesting structural aspect of the Id2 NES region, which might be of significance for both protein folding and function. (c) 2006 Elsevier Inc. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | LOOP-HELIX PROTEINS; TRANSCRIPTION FACTORS; CELL-GROWTH; FAMILY; DIFFERENTIATION; PHOSPHORYLATION; TUMORIGENESIS; REGULATOR; CANCER; CYCLE; nuclear export signal; Id2 protein; fibrils; circular dichroism; electron microscopy; peptide aggregation |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Pathologie Chemistry and Pharmacy > Institut für Organische Chemie > Alumni or Retired Professors > Arbeitskreis Dr. Chiara Cabrele |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 09 Feb 2021 14:53 |
| Last Modified: | 09 Feb 2021 14:53 |
| URI: | https://pred.uni-regensburg.de/id/eprint/34289 |
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