Identification of a transactivation motif in the CLN3 protein.
A transactivation motif has been identified in the neurodegenerative disease protein, CLN3. The C-terminal domain (residues 394-438) of CLN3 can function as a transcriptional activator when fused to the DNA binding domain, LexA. A series of deletion and substitution constructs have been generated to identify the essential region for transactivation. A similar motif is also present in the POU domain transcription factor, nubbin. However, this domain alone does not activate transcription, allowing further localisation of the critical residues in CLN3 required for activity.
Leung
K Y
KY
Department of Paediatrics, Royal Free and University College London Medical School, Rayne Institute, United Kingdom. kit-yi.leung@harefield.nthames.nhs.uk
Greene
N D
ND
Munroe
P B
PB
Mole
S E
SE
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics; D017930:Genes, Reporter; D006801:Humans; D066298:In Vitro Techniques; D007763:Lac Operon; D008562:Membrane Glycoproteins; D018832:Molecular Chaperones; D008969:Molecular Sequence Data; D009472:Neuronal Ceroid-Lipofuscinoses / Q000235:genetics; D011506:Proteins / Q000737:chemistry / Q000235:genetics*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000235:genetics; D012697:Serine Endopeptidases / Q000737:chemistry / Q000235:genetics; D015533:Transcriptional Activation; D020798:Two-Hybrid System Techniques; D000099160:LexA Repressor Protein
D001426:Bacterial Proteins; D008562:Membrane Glycoproteins; D018832:Molecular Chaperones; D011506:Proteins; D011993:Recombinant Fusion Proteins; D012697:Serine Endopeptidases; D000099160:LexA Repressor Protein; C105199:CLN3 protein, human