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

• Type of Material: Article
• Authors: Simona Cugusi, Emory University; Satish Kallappagoudar, Emory University; Huiping Ling, Emory University; John Lucchesi, Emory University
• Language: English
• Date: 2015-06
• Publisher: American Society for Biochemistry and Molecular Biology
• Publication Version: Final Published Version
• Copyright Statement: © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
• License: Creative Commons Attribution 3.0 Unported
• Final Published Version (URL): http://dx.doi.org/10.1074/mcp.M114.040667
• Title of Journal or Parent Work: Molecular & Cellular Proteomics
• ISSN: 1535-9476
• Volume: 14
• Issue: 6
• Start Page: 1478
• End Page: 1488
• Grant/Funding Information: 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.; This work was partially funded by National Institutes of Health grant GM15691 to JCL.
• Research Categories: Biology, Molecular; Chemistry, Biochemistry

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.