Translation controlled 英文参考文献.docVIP

Meeting report Translation controlled Graham D Pavitt and Mark P Ashe Address: Faculty of Life Sciences, The University of Manchester, Manchester M13 9PT, UK. Correspondence: Graham D Pavitt. Email: graham.pavitt@manchester.ac.uk; Mark P Ashe. Email: mark.ashe@manchester.ac.uk. Published: 21 October 2008 Genome Biology 2008, 9:323 (doi:10.1186/gb-2008-9-10-323) The electronic version of this article is the complete one and can be found online at /2008/9/10/323 ? 2008 BioMed Central Ltd protein, DHX29, is a DExH-domain protein with putative A report of the meeting ‘Translational Control’, Cold Spring ATP-dependent RNA helicase activity. Although little Harbor, USA, 3-7 September 2008. evidence for helicase activity was found, the protein was shown to associate with the small ribosomal subunit and to possess nucleotide triphosphatase (NTPase) activity. DHX29 was also shown to promote efficient recruitment of the small ribosomal subunit to structured 5′ UTR mRNAs in a manner that is synergistic with eIF4A, defining DHX29 as a novel factor required for scanning on structured 5′ UTRs. More than 400 scientists contributed to this year’s highly successful ‘Translational control’ meeting at the Cold Spring Harbor Laboratory. Translation is a complex and highly regulated multi-step process, fundamental to all forms of life. The meeting covered a diverse range of topics, experi- mental systems and approaches. Here we report a few of the highlights from the major themes of the meeting, focusing mainly on contributions not published at the time of writing. Nancy Standart (University of Cambridge, UK) presented a mutational analysis targeting the helicase domain of the protein DDX6 (also called p54 and Dhh1 in different organisms). DDX6 has been described as a translational repressor (for instance as part of the cytoplasmic poly- adenylation element bind