Abstract

DEAD-box proteins comprise a family of ATP-dependent RNA helicases involved in several aspects of RNA metabolism. Here we report the characterization of the human DEAD-box RNA helicase DDX26. The gene is composed of 14 exons distributed over an extension of 8,123 bp of genomic sequence and encodes a transcript of 1.8 kb that is expressed in all tissues evaluated. The predicted amino acid sequence shows a high similarity to a yeast DEAD-box RNA helicase (Dbp9b) involved in ribosome biogenesis. The new helicase maps to 7p12, a region of frequent chromosome amplifications in glioblastomas involving the epidermal growth factor receptor (EGFR) gene. Nevertheless, co-amplification of DDX26 with EGFR was not detected in nine tumors analyzed.

Highlights

  • Helicases, including DNA and RNA helicases, are grouped into two major superfamilies of proteins (SFI and SFII) on the basis of the occurrence of conserved motifs [1]

  • DEAD-box RNA helicases are characterized by the presence of eight conserved motifs including an RNA interaction domain and an ATP hydrolysis motif containing the core amino acid sequence DEAD [2]

  • Cancer Genome Project [9], we identified an EST with significant similarity to a DEADbox RNA helicase from yeast and various other organisms as well as to a finished human genomic sequence corresponding to the PAC clone DJ0971C03 (AC004938)

Read more

Summary

Introduction

Helicases, including DNA and RNA helicases, are grouped into two major superfamilies of proteins (SFI and SFII) on the basis of the occurrence of conserved motifs [1]. RNA helicases are mostly of the SFII superfamily and can be further classified into families on the basis of particular consensus sequences in the conserved ATP hydrolysis motif. In contrast to DNA helicases, which processively unwind long regular dsDNA structures, most RNA helicases modulate only short duplex regions in RNA molecules in a one-step reaction in the presence of ATP [1]. DEAD-box RNA helicases are characterized by the presence of eight conserved motifs including an RNA interaction domain and an ATP hydrolysis motif containing the core amino acid sequence DEAD [2]. In addition to the conserved motifs, RNA helicases contain variable N and C terminal extensions that might confer substrate specificity and/or contain information directing subcellular localization [3]

Methods
Results
Conclusion

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.