A new Resource for Nature Structural and Molecular Biology
Nature Structural & Molecular Biology (15, 767; 2008) announces a new section of the journal for articles that serve primarily as resources and also lead to novel molecular insights. Nature Structural & Molecular Biology focuses on the underpinnings of biological processes at the molecular level. However, in this era of large-scale, high-throughput experimentation, an increasing number of submissions to the journal describe mammoth data sets and the tools that facilitate their analysis. The new Resource section is for analyses of new data sets that lead to novel and arresting conclusions, as described in the journal's Guide to Authors. Resources are broad in scope and, in an era of burgeoning and ever-expanding technological advances, the approaches and findings that characterize this section will undoubtedly change over time. There are two examples of Resource articles in the journal's August issue:
Fission yeast SWI/SNF and RSC complexes show compositional and functional differences from budding yeast pp873 - 880
Brendon J Monahan, Judit Villén, Samuel Marguerat, Jurg Bahler, Steven P Gygi and Fred Winston
The Schizosaccharomyces pombe SWI/SNF family of ATP-dependent chromatin-remodeling complexes is now comprehensively analyzed, through composition, phenotypic and microarray analyses, thus broadly setting the stage for S. pombe as a new model organism for examining the SWI/SNF family remodelers. The S. pombe complexes are more akin to the metazoan SWI/SNF remodelers and have specific roles in repression of iron-transport genes.
A comprehensive library of histone mutants identifies nucleosomal residues required for H3K4 methylation pp881 - 888 Shima Nakanishi, Brian W Sanderson, Kym M Delventhal, William D Bradford, Karen Staehling-Hampton and Ali Shilatifard
A comprehensive library encompassing alanine scanning mutations across yeast histones is presented as a Resource that will facilitate screening of chromatin processes. The utility of the library is indicated by screening in cis and in trans for residues that affect histone H3K4 trimethylation, a modification that is associated with actively transcribed genes and known to be mediated by the Set1-COMPASS complex.
