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  IGHMBP2 is a ribosome-associated helicase inactive in the neuromuscular disorder distal SMA type 1 (DSMA1)

Guenther, U.-P., Handoko, L., Laggerbauer, B., Jablonka, S., Chari, A., Alzheimer, M., et al. (2009). IGHMBP2 is a ribosome-associated helicase inactive in the neuromuscular disorder distal SMA type 1 (DSMA1). Human Molecular Genetics, 18(7), 1288-1300. doi:10.1093/hmg/ddp028.

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3287419.pdf (Publisher version), 524KB
 
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Guenther, U.-P., Author
Handoko, L., Author
Laggerbauer, B., Author
Jablonka, S., Author
Chari, A.1, Author           
Alzheimer, M., Author
Ohmer, J., Author
Plöttner, O., Author
Gehring, N., Author
Sickmann, A., Author
von Au, K., Author
Schuelke, M., Author
Fischer, U., Author
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1Research Group of Structural Biochemistry and Mechanisms, MPI for Biophysical Chemistry, Max Planck Society, ou_3265855              

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Free keywords: neuromuscular diseases, mutation, adenosine triphosphatases, cytoplasm, dna, ribosomes, mice, rna INTRODUCTION
 Abstract: Distal spinal muscular atrophy type 1 (DSMA1) is an autosomal recessive disease that is clinically characterized by distal limb weakness and respiratory distress. In this disease, the degeneration of α-motoneurons is caused by mutations in the immunoglobulin μ-binding protein 2 (IGHMBP2). This protein has been implicated in DNA replication, pre-mRNA splicing and transcription, but its precise function in all these processes has remained elusive. We have purified catalytically active recombinant IGHMBP2, which has enabled us to assess its enzymatic properties and to identify its cellular targets. Our data reveal that IGHMBP2 is an ATP-dependent 5′→3′ helicase, which unwinds RNA and DNA duplices in vitro. Importantly, this helicase localizes predominantly to the cytoplasm of neuronal and non-neuronal cells and associates with ribosomes. DSMA1-causing amino acid substitutions in IGHMBP2 do not affect ribosome binding yet severely impair ATPase and helicase activity. We propose that IGHMBP2 is functionally linked to translation, and that mutations in its helicase domain interfere with this function in DSMA1 patients.

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Language(s): eng - English
 Dates: 2009-01-202009-04-01
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1093/hmg/ddp028
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Title: Human Molecular Genetics
Source Genre: Journal
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Pages: - Volume / Issue: 18 (7) Sequence Number: - Start / End Page: 1288 - 1300 Identifier: -