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Author Notes:

Correspondence: John C. Lucchesi, Department of Biology, Emory University, Atlanta, GA 30322. Email: jclucch@emory.edu.

S.C., S.K., and J.C.L. designed research.

S.C., S.K., and H.L. performed research.

S.C. analyzed data.

S.C. and J.C.L. wrote the paper.

We thank Drs. C. P. Verrijzer, H. Saumweber and R. Nusse for their gifts of antibodies, and Drs. S. Artavanis-Tsakonas and K.D. Irvine for their gifts of plasmids.

We are grateful to Dr. Ashok Reddy, associate director of the OHSU proteomics core for his help with the MS data.

We also thank Dr. Paul Wade for his very useful comments on the manuscript.

Subjects:

Research Funding:

This work was partially funded by National Institutes of Health grant GM15691 to JCL.

Mass spectrometric analysis was performed by the OHSU Proteomics Shared Resource with partial support from NIH core grants P30EY010572, P30CA069533, S10OD012246, S10RR025571, and R01DC002368-15S1.

The Drosophila Helicase Maleless (MLE) is Implicated in Functions Distinct From its Role in Dosage Compensation

Journal Title:

Molecular & Cellular Proteomics

Volume:

Volume 14, Number 6

Publisher:

, Pages 1478-1488

Type of Work:

Article | Final Publisher PDF

Abstract:

Helicases are ubiquitous enzymes that unwind or remodel single or double-stranded nucleic acids, and that participate in a vast array of metabolic pathways. The ATP-dependent DEXH-box RNA/DNA helicase MLE was first identified as a core member of the chromatin remodeling MSL complex, responsible for dosage compensation in Drosophila males. Although this complex does not assemble in females, MLE is present. Given the multiplicity of functions attributed to its mammalian ortholog RNA helicase A, we have carried out an analysis for the purpose of determining whether MLE displays the same diversity. We have identified a number of different proteins that associate with MLE, implicating its role in specific pathways. We have documented this association in selected examples that include the spliceosome complex, heterogeneous Nuclear Ribonucleoproteins involved in RNA Processing and in Heterochromatin Protein 1 deposition, and the NuRD complex.

Copyright information:

© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

This is an Open Access article distributed under the terms of the Creative Commons Attribution 3.0 Unported License ( http://creativecommons.org/licenses/by/3.0/), which permits distribution, public display, and publicly performance, making multiple copies, distribution of derivative works, provided the original work is properly cited. This license requires credit be given to copyright holder and/or author, copyright and license notices be kept intact.

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