Open AccessPreliminary crystallographic analysis of a possible transcription factor encoded by the mimivirus L544 gene
Author(s) -
Ciaccafava Alexandre,
Lartigue Audrey,
Mansuelle Pascal,
Jeudy Sandra,
Abergel Chantal
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111020847
Subject(s) - biology , transcription (linguistics) , gene , recombinant dna , virology , rna polymerase , rna , genetics , philosophy , linguistics
Mimivirus is the prototype of a new family (the Mimiviridae ) of nucleocytoplasmic large DNA viruses (NCLDVs), which already include the Poxviridae , Iridoviridae , Phycodnaviridae and Asfarviridae . Mimivirus specifically replicates in cells from the genus Acanthamoeba . Proteomic analysis of purified mimivirus particles revealed the presence of many subunits of the DNA‐directed RNA polymerase II complex. A fully functional pre‐transcriptional complex appears to be loaded in the virions, allowing mimivirus to initiate transcription within the host cytoplasm immediately upon infection independently of the host nuclear apparatus. To fully understand this process, a systematic study of mimivirus proteins that are predicted (by bioinformatics) or suspected (by proteomic analysis) to be involved in transcription was initiated by cloning and expressing them in Escherichia coli in order to determine their three‐dimensional structures. Here, preliminary crystallographic analysis of the recombinant L544 protein is reported. The crystals belonged to the orthorhombic space group C 222 1 with one monomer per asymmetric unit. A MAD data set was used for preliminary phasing using the selenium signal present in a selenomethionine‐substituted protein crystal.