Identification of a Transactivation Motif in the CLN3 Protein

• Published in: IUBMB life Vol. 51; no. 5; pp. 295 - 298
• Main Authors: Leung, K. Y., Greene, N. D. E., Munroe, P. B., Mole, S. E.
• Format: Journal Article
• Language: English
• Published: UK Informa Healthcare 01-05-2001
• Subjects: Activation; Amino Acid Motifs; Amino Acid Sequence; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Cln3; Domain; Factor; Genes, Reporter; Humans; In Vitro Techniques; Lac Operon; Membrane Glycoproteins; Molecular Chaperones; Molecular Sequence Data; Neuronal Ceroid-Lipofuscinoses - genetics; Proteins - chemistry; Proteins - genetics; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - genetics; Saccharomyces cerevisiae - genetics; Serine Endopeptidases - chemistry; Serine Endopeptidases - genetics; Transcription; Transcriptional Activation; Two-Hybrid System Techniques; Yeast‐ONE‐HYBRID
• ISSN: 1521-6543; 1521-6551
• DOI: 10.1080/152165401317190798

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.