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Statements

Subject Item
n2:RIV%2F00216208%3A11310%2F11%3A10104589%21RIV12-MSM-11310___
rdf:type
skos:Concept n12:Vysledek
rdfs:seeAlso
http://dx.doi.org/10.1371/journal.pone.0023650
dcterms:description
Background: CSL (CBF1/RBP-J kappa/Suppressor of Hairless/LAG-1) transcription factors are the effector components of the Notch receptor signalling pathway, which is critical for metazoan development. The metazoan CSL proteins (class M) can also function in a Notch-independent manner. Recently, two novel classes of CSL proteins, designated F1 and F2, have been identified in fungi. The role of the fungal CSL proteins is unclear, because the Notch pathway is not present in fungi. In fission yeast, the Cbf11 and Cbf12 CSL paralogs play antagonistic roles in cell adhesion and the coordination of cell and nuclear division. Unusually long N-terminal extensions are typical for fungal and invertebrate CSL family members. In this study, we investigate the functional significance of these extended N-termini of CSL proteins. Methodology/Principal Findings: We identify 15 novel CSL family members from 7 fungal species and conduct bioinformatic analyses of a combined dataset containing 34 fungal and 11 metazoan CSL protein sequences. We show that the long, non-conserved N-terminal tails of fungal CSL proteins are likely disordered and enriched in phosphorylation sites and PEST motifs. In a case study of Cbf12 (class F2), we provide experimental evidence that the protein is proteolytically processed and that the N-terminus inhibits the Cbf12-dependent DNA binding activity in an electrophoretic mobility shift assay. Conclusions/Significance: This study provides insight into the characteristics of the long N-terminal tails of fungal CSL proteins that may be crucial for controlling DNA-binding and CSL function. We propose that the regulation of DNA binding by Cbf12 via its N-terminal region represents an important means by which fission yeast strikes a balance between the class F1 and class F2 paralog activities. This mode of regulation might be shared with other CSL-positive fungi, some of which are relevant to human disease and biotechnology. Background: CSL (CBF1/RBP-J kappa/Suppressor of Hairless/LAG-1) transcription factors are the effector components of the Notch receptor signalling pathway, which is critical for metazoan development. The metazoan CSL proteins (class M) can also function in a Notch-independent manner. Recently, two novel classes of CSL proteins, designated F1 and F2, have been identified in fungi. The role of the fungal CSL proteins is unclear, because the Notch pathway is not present in fungi. In fission yeast, the Cbf11 and Cbf12 CSL paralogs play antagonistic roles in cell adhesion and the coordination of cell and nuclear division. Unusually long N-terminal extensions are typical for fungal and invertebrate CSL family members. In this study, we investigate the functional significance of these extended N-termini of CSL proteins. Methodology/Principal Findings: We identify 15 novel CSL family members from 7 fungal species and conduct bioinformatic analyses of a combined dataset containing 34 fungal and 11 metazoan CSL protein sequences. We show that the long, non-conserved N-terminal tails of fungal CSL proteins are likely disordered and enriched in phosphorylation sites and PEST motifs. In a case study of Cbf12 (class F2), we provide experimental evidence that the protein is proteolytically processed and that the N-terminus inhibits the Cbf12-dependent DNA binding activity in an electrophoretic mobility shift assay. Conclusions/Significance: This study provides insight into the characteristics of the long N-terminal tails of fungal CSL proteins that may be crucial for controlling DNA-binding and CSL function. We propose that the regulation of DNA binding by Cbf12 via its N-terminal region represents an important means by which fission yeast strikes a balance between the class F1 and class F2 paralog activities. This mode of regulation might be shared with other CSL-positive fungi, some of which are relevant to human disease and biotechnology.
dcterms:title
N-Termini of Fungal CSL Transcription Factors Are Disordered, Enriched in Regulatory Motifs and Inhibit DNA Binding in Fission Yeast N-Termini of Fungal CSL Transcription Factors Are Disordered, Enriched in Regulatory Motifs and Inhibit DNA Binding in Fission Yeast
skos:prefLabel
N-Termini of Fungal CSL Transcription Factors Are Disordered, Enriched in Regulatory Motifs and Inhibit DNA Binding in Fission Yeast N-Termini of Fungal CSL Transcription Factors Are Disordered, Enriched in Regulatory Motifs and Inhibit DNA Binding in Fission Yeast
skos:notation
RIV/00216208:11310/11:10104589!RIV12-MSM-11310___
n12:predkladatel
n13:orjk%3A11310
n3:aktivita
n8:S n8:P n8:Z
n3:aktivity
P(LC07032), S, Z(MSM0021620858)
n3:cisloPeriodika
8
n3:dodaniDat
n15:2012
n3:domaciTvurceVysledku
n9:2714175 n9:8000964 n9:6816878 n9:8168768
n3:druhVysledku
n7:J
n3:duvernostUdaju
n16:S
n3:entitaPredkladatele
n22:predkladatel
n3:idSjednocenehoVysledku
216712
n3:idVysledku
RIV/00216208:11310/11:10104589
n3:jazykVysledku
n21:eng
n3:klicovaSlova
phosphorylation; fungi; CSL family; Schizosaccharomyces pombe; fission yeast; proteolysis; PEST motif; DNA binding; protein disorder; transcription factor
n3:klicoveSlovo
n5:phosphorylation n5:proteolysis n5:protein%20disorder n5:DNA%20binding n5:CSL%20family n5:fungi n5:PEST%20motif n5:Schizosaccharomyces%20pombe n5:fission%20yeast n5:transcription%20factor
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[F05BB57EDA0B]
n3:nazevZdroje
PLoS ONE
n3:obor
n4:EB
n3:pocetDomacichTvurcuVysledku
4
n3:pocetTvurcuVysledku
8
n3:projekt
n20:LC07032
n3:rokUplatneniVysledku
n15:2011
n3:svazekPeriodika
6
n3:tvurceVysledku
Ptáčková, Martina Gould, Kathleen Baehler, Juerg McLean, Janel R Atkinson, Sophie R Převorovský, Martin Folk, Petr Půta, František
n3:wos
000293953500059
n3:zamer
n18:MSM0021620858
s:issn
1932-6203
s:numberOfPages
11
n17:doi
10.1371/journal.pone.0023650
n14:organizacniJednotka
11310