Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bbrc.2007.12.022
Title: A novel nucleolar transcriptional activator ApLLP for long-term memory formation is intrinsically unstructured but functionally active
Authors: Liu, J. 
Song, J. 
Keywords: ApLLP
Aplysia
Circular dichroism
DNA-binding
Intrinsically unstructured protein (IUP)
Long-term memory
Neuron
NMR spectroscopy
Nucleolar transcriptional activator
Short-term memory
Issue Date: 2008
Source: Liu, J., Song, J. (2008). A novel nucleolar transcriptional activator ApLLP for long-term memory formation is intrinsically unstructured but functionally active. Biochemical and Biophysical Research Communications 366 (2) : 585-591. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbrc.2007.12.022
Abstract: A novel Aplysia nucleolar protein ApLLP has been recently characterized to be a transcriptional activator that binds to the cAMP-response element (CRE) and thus induces ApC/EBP expression required for establishing long-term memory. So far, no structural information is available for both ApLLP and its homologs. Here, we expressed the entire ApLLP and its two dissected fragments, followed by structural and binding studies using CD and NMR spectroscopy. The study leads to two interesting findings: (1) all three ApLLP proteins are highly disordered, owning no predominant secondary and tertiary structures; (2) ApLLP is capable of binding the CRE DNA element but this induces no significant change in its secondary and tertiary structures. Intriguingly, it appears that the DNA-binding residues are mainly located on the C-half of the ApLLP molecule. Taken together, our results define ApLLP as an intrinsically unstructured protein and may bear important implications in understanding the molecular mechanism underlying ApLLP functions. © 2007 Elsevier Inc. All rights reserved.
Source Title: Biochemical and Biophysical Research Communications
URI: http://scholarbank.nus.edu.sg/handle/10635/28790
ISSN: 0006291X
10902104
DOI: 10.1016/j.bbrc.2007.12.022
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