In this article we are going to delve into the topic of DDX5, exploring its origins, its impact on society and its relevance today. DDX5 has been the subject of study and debate for many years, and its influence extends to different areas of everyday life, from culture to politics and technology. Throughout these pages, we will take a closer look at the different aspects of DDX5, and how it has evolved over time. Additionally, we will examine its role in shaping our world today and how it could impact the future. Get ready to immerse yourself in a fascinating journey through DDX5 and discover everything there is to know about this topic.
Probable ATP-dependent RNA helicase DDX5 also known as DEAD box protein 5 or RNA helicase p68 is an enzyme that in humans is encoded by the DDX5gene.[5]
Function
DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure, such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis,[6] and cellular growth and division. This gene encodes a DEAD box protein, which is an RNA-dependent ATPase, and also a proliferation-associated nuclear antigen, specifically reacting with the simian virus 40 tumor antigen. This gene consists of 13 exons, and alternatively spliced transcripts containing several intron sequences have been detected, but no isoforms encoded by these transcripts have been identified.[5]
^Nicol SM, Causevic M, Prescott AR, Fuller-Pace FV (June 2000). "The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase". Exp. Cell Res. 257 (2): 272–80. doi:10.1006/excr.2000.4886. PMID10837141.
Nicol SM, Causevic M, Prescott AR, Fuller-Pace FV (2000). "The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase". Exp. Cell Res. 257 (2): 272–80. doi:10.1006/excr.2000.4886. PMID10837141.