TAILIEUCHUNG - Báo cáo khoa học: Analysis of Lsm1p and Lsm8p domains in the cellular localization of Lsm complexes in budding yeast

In eukaryotes, two heteroheptameric Sm-like (Lsm) complexes that differ by a single subunit localize to different cellular compartments and have dis-tinct functions in RNA metabolism. The cytoplasmic Lsm1–7p complex promotes mRNA decapping and localizes to processing bodies, whereas the Lsm2–8p complex takes part in a variety of nuclear RNA processing events. | ễFEBS Journal Analysis of Lsmlp and Lsm8p domains in the cellular localization of Lsm complexes in budding yeast Martin A. M. Reijns Tatsiana Auchynnikava and Jean D. Beggs Wellcome Trust Centre for CellBiology University of Edinburgh UK Keywords Lsm1-7p Lsm2-8p nuclear localization P-bodies Saccharomyces cerevisiae Correspondence J. D. Beggs Wellcome Trust Centre for Cell Biology University of Edinburgh King s Buildings Mayfield Road Edinburgh EH9 3JR UK Fax 44 131 650 8650 Tel 44 131 650 5351 E-mail jbeggs@ Present address Medical Research Council Human Genetics Unit Western General Hospital Edinburgh UK Received 29 December 2008 revised 28 April 2009 accepted 30 April 2009 doi In eukaryotes two heteroheptameric Sm-like Lsm complexes that differ by a single subunit localize to different cellular compartments and have distinct functions in RNA metabolism. The cytoplasmic Lsm1-7p complex promotes mRNA decapping and localizes to processing bodies whereas the Lsm2-8p complex takes part in a variety of nuclear RNA processing events. The structural features that determine their different functions and localizations are not known. Here we analyse a range of mutant and hybrid Lsm1 and Lsm8 proteins shedding light on the relative importance of their various domains in determining their localization and ability to support growth. Although no single domain is either essential or sufficient for cellular localization the Lsm1p N-terminus may act as part of a nuclear exclusion signal for Lsm1-7p and the shorter Lsm8p N-terminus contributes to nuclear accumulation of Lsm2-8p. The C-terminal regions seem to play a secondary role in determining localization with little or no contribution coming from the central Sm domains. The essential Lsm8 protein is remarkably resistant to mutation in terms of supporting viability whereas Lsm1p appears more sensitive. These findings contribute to our understanding of how two very similar protein .

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