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          Institute: MPI für Entwicklungsbiologie     Collection: Abteilung 2 - Biochemistry (E. Izaurralde)     Display Documents



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ID: 695230.0, MPI für Entwicklungsbiologie / Abteilung 2 - Biochemistry (E. Izaurralde)
Structure and properties of the esterase from non-LTR retrotransposons suggest a role for lipids in retrotransposition
Authors:Schneider, A. M.; Schmidt, S.; Jonas, S.; Vollmer, B.; Khazina, E.; Weichenrieder, O.
Date of Publication (YYYY-MM-DD):2013-12
Title of Journal:Nucleic Acids Research
Journal Abbrev.:Nucleic Acids Res
Volume:41
Issue / Number:22
Start Page:10563
End Page:10572
Sequence Number of Article:24003030
Review Status:Internal review
Audience:Experts Only
Abstract / Description:Non-LTR retrotransposons are mobile genetic elements and play a major role in eukaryotic genome evolution and disease. Similar to retroviruses they encode a reverse transcriptase, but their genomic integration mechanism is fundamentally different, and they lack homologs of the retroviral nucleocapsid-forming protein Gag. Instead, their first open reading frames encode distinct multi-domain proteins (ORF1ps) presumed to package the retrotransposon-encoded RNA into ribonucleoprotein particles (RNPs). The mechanistic roles of ORF1ps are poorly understood, particularly of ORF1ps that appear to harbor an enzymatic function in the form of an SGNH-type lipolytic acetylesterase. We determined the crystal structures of the coiled coil and esterase domains of the ORF1p from the Danio rerio ZfL2-1 element. We demonstrate a dimerization of the coiled coil and a hydrolytic activity of the esterase. Furthermore, the esterase binds negatively charged phospholipids and liposomes, but not oligo-(A) RNA. Unexpectedly, the esterase can split into two dynamic half-domains, suited to engulf long fatty acid substrates extending from the active site. These properties indicate a role for lipids and membranes in non-LTR retrotransposition. We speculate that Gag-like membrane targeting properties of ORF1ps could play a role in RNP assembly and in membrane-dependent transport or localization processes.
Free Keywords:Amino Acid Sequence; Animals; Esterases/*chemistry/genetics/metabolism; Fatty Acids/chemistry; Liposomes; Models, Molecular; Molecular Sequence Data; Phospholipids/metabolism; Protein Multimerization; Protein Structure, Tertiary; *Retroelements; Zebrafish/genetics; Zebrafish Proteins/*chemistry/genetics/metabolism
External Publication Status:published
Document Type:Article
Communicated by:root
Affiliations:MPI für Entwicklungsbiologie/Abteilung 2 - Biochemie (Elisa Izaurralde)
Identifiers:ISSN:1362-4962 (Electronic) 0305-1048 (Linking) %R 10.1... [ID No:1]
URL:http://www.ncbi.nlm.nih.gov/pubmed/24003030 [ID No:2]
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