The Leucine Zipper Domains of the Transcription Factors GCN4 and c-Jun Have Ribonuclease Activity

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Author(s) Nikolaev, Yaroslav, Deillon, Christine, Hoffmann, Stefan R.K., Bigler, Laurent, Friess, Sebastian, Zenobi, Renato, Pervushin, Konstantin, Hunziker, Peter, Gutte, Bernd
Publication Type Journal Items, Publication Status: Published
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Title The Leucine Zipper Domains of the Transcription Factors GCN4 and c-Jun Have Ribonuclease Activity
Author(s) Nikolaev, Yaroslav
Deillon, Christine
Hoffmann, Stefan R.K.
Bigler, Laurent
Friess, Sebastian
Zenobi, Renato
Pervushin, Konstantin
Hunziker, Peter
Gutte, Bernd
Description 12 p.
Journal or Series Title PLoS ONE
Volume Number 5
Issue Number 5
Start Page e10765
ISSN 1932-6203
Publisher Public Library of Science
Publication Place Lawrence, KS
Publication Date 2010
Abstract Basic-region leucine zipper (bZIP) proteins are one of the largest transcription factor families that regulate a wide range of cellular functions. Owing to the stability of their coiled coil structure leucine zipper (LZ) domains of bZIP factors are widely employed as dimerization motifs in protein engineering studies. In the course of one such study, the X-ray structure of the retro-version of the LZ moiety of yeast transcriptional activator GCN4 suggested that this retro-LZ may have ribonuclease activity. Here we show that not only the retro-LZ but also the authentic LZ of GCN4 has weak but distinct ribonuclease activity. The observed cleavage of RNA is unspecific, it is not suppressed by the ribonuclease A inhibitor RNasin and involves the breakage of 3′,5′-phosphodiester bonds with formation of 2′,3′-cyclic phosphates as the final products as demonstrated by HPLC/electrospray ionization mass spectrometry. Several mutants of the GCN4 leucine zipper are catalytically inactive, providing important negative controls and unequivocally associating the enzymatic activity with the peptide under study. The leucine zipper moiety of the human factor c-Jun as well as the entire c-Jun protein are also shown to catalyze degradation of RNA. The presented data, which was obtained in the test-tube experiments, adds GCN4 and c-Jun to the pool of proteins with multiple functions (also known as moonlighting proteins). If expressed in vivo, the endoribonuclease activity of these bZIP-containing factors may represent a direct coupling between transcription activation and controlled RNA turnover. As an additional result of this work, the retro-leucine zipper of GCN4 can be added to the list of functional retro-peptides.
DOI 10.1371/journal.pone.0010765
Additional Notes Received 25 September 2009, Accepted 26 April 2010, Published 21 May 2010
Document Type Article
Publication Status Published
Language English
Assigned Organisational Unit(s) 02207
03430
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Source Database ID FORM-1275378243
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@article{Nklv2010,
  author = "Nikolaev, Yaroslav and Deillon, Christine and Hoffmann, Stefan R.K. and Bigler, Laurent and Friess, Sebastian and Zenobi, Renato and Pervushin, Konstantin and Hunziker, Peter and Gutte, Bernd",
  title = "{T}he {L}eucine {Z}ipper {D}omains of the {T}ranscription {F}actors {G}{C}{N}4 and c-{J}un {H}ave {R}ibonuclease {A}ctivity",
  journal = "PLoS ONE",
  year = 2010,
  volume = "5",
  number = "5",
  pages = "e10765--",
}


E-Citations record created: Tue, 01 Jun 2010, 07:44:08 CET