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Title: The Survival Motor Neuron Protein Forms Soluble Glycine Zipper Oligomers

Abstract

The survival motor neuron (SMN) protein forms the oligomeric core of a multiprotein complex that functions in spliceosomal snRNP biogenesis. Loss of function mutations in the SMN gene cause spinal muscular atrophy (SMA), a leading genetic cause of infant mortality. Nearly half of the known SMA patient missense mutations map to the SMN YG-box, a highly conserved oligomerization domain of unknown structure that contains a (YxxG)3 motif. Here, we report that the SMN YG-box forms helical oligomers similar to the glycine zippers found in transmembrane channel proteins. A network of tyrosine-glycine packing between helices drives formation of soluble YG-box oligomers, providing a structural basis for understanding SMN oligomerization and for relating defects in oligomerization to the mutations found in SMA patients. These results have important implications for advancing our understanding of SMN function and glycine zipper-mediated helix-helix interactions.

Authors:
; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
OTHERNIGMS
OSTI Identifier:
1054369
Resource Type:
Journal Article
Journal Name:
Structure
Additional Journal Information:
Journal Volume: 20; Journal Issue: 11; Journal ID: ISSN 0969-2126
Publisher:
Elsevier
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Martin, Renee, Gupta, Kushol, Ninan, Nisha S., Perry, Kay, and Van Duyne, Gregory D. The Survival Motor Neuron Protein Forms Soluble Glycine Zipper Oligomers. United States: N. p., 2012. Web. doi:10.1016/j.str.2012.08.024.
Martin, Renee, Gupta, Kushol, Ninan, Nisha S., Perry, Kay, & Van Duyne, Gregory D. The Survival Motor Neuron Protein Forms Soluble Glycine Zipper Oligomers. United States. doi:10.1016/j.str.2012.08.024.
Martin, Renee, Gupta, Kushol, Ninan, Nisha S., Perry, Kay, and Van Duyne, Gregory D. Thu . "The Survival Motor Neuron Protein Forms Soluble Glycine Zipper Oligomers". United States. doi:10.1016/j.str.2012.08.024.
@article{osti_1054369,
title = {The Survival Motor Neuron Protein Forms Soluble Glycine Zipper Oligomers},
author = {Martin, Renee and Gupta, Kushol and Ninan, Nisha S. and Perry, Kay and Van Duyne, Gregory D.},
abstractNote = {The survival motor neuron (SMN) protein forms the oligomeric core of a multiprotein complex that functions in spliceosomal snRNP biogenesis. Loss of function mutations in the SMN gene cause spinal muscular atrophy (SMA), a leading genetic cause of infant mortality. Nearly half of the known SMA patient missense mutations map to the SMN YG-box, a highly conserved oligomerization domain of unknown structure that contains a (YxxG)3 motif. Here, we report that the SMN YG-box forms helical oligomers similar to the glycine zippers found in transmembrane channel proteins. A network of tyrosine-glycine packing between helices drives formation of soluble YG-box oligomers, providing a structural basis for understanding SMN oligomerization and for relating defects in oligomerization to the mutations found in SMA patients. These results have important implications for advancing our understanding of SMN function and glycine zipper-mediated helix-helix interactions.},
doi = {10.1016/j.str.2012.08.024},
journal = {Structure},
issn = {0969-2126},
number = 11,
volume = 20,
place = {United States},
year = {2012},
month = {11}
}