@article{mbs:/content/journal/jgv/10.1099/0022-1317-75-6-1345, author = "Müller, R. and Poch, O. and Delarue, M. and Bishop, D. H. L. and Bouloy, M.", title = "Rift valley fever virus L segment: correction of the sequence and possible functional role of newly identified regions conserved in RNA-dependent polymerases", journal= "Journal of General Virology", year = "1994", volume = "75", number = "6", pages = "1345-1352", doi = "https://doi.org/10.1099/0022-1317-75-6-1345", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-75-6-1345", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The sequence of Rift Valley fever virus L segment that we published in a previous paper was erroneous in the 3′ -terminal region of the antigenomic RNA molecule. Here, we have shown that the L segment is in fact 6404 nucleotides long and encodes a polypeptide of 237·7K in the viral complementary sense. Sequence comparisons performed between the RNA-dependent RNA polymerases of 22 negative-stranded RNA viruses revealed the existence of two novel regions located at the amino termini of the proteins and conserved only in the polymerases of bunya- and arenaviruses. In the region conserved in all RNA-dependent polymerases, corresponding to the so-called ‘polymerase module’, we identified a new motif, designated premotif A, common to all RNA-dependent polymerases, as well as amino acids located in the region between motifs preA and A which are strictly conserved for segmented negative- stranded RNA viruses. Using the recently released coordinates of human immunodeficiency virus reverse transcriptase and the alignment between all RNA- dependent polymerases in the ‘polymerase module’, we have determined the position of the conserved residues in these polymerases and discuss their possible functions in light of the available structural information.", }