Nature Structural & Molecular Biology - AOP - nature.com science feeds Nature Structural & Molecular Biology is an integrated forum for structural and molecular studies. The journal places a strong emphasis on functional and mechanistic understanding of how molecular components in a biological process work together. Structural data may provide such insights, but they are not a pre-requisite for publication in the journal. http://www.nature.com/nsmb/current_issue/ Nature Publishing Group en © Nature Publishing Group Nature Structural & Molecular Biology 1545-9993 1545-9985 © Nature Publishing Group permissions@nature.com Nature Structural & Molecular Biology http://www.nature.com/includes/rj_globnavimages/nsmb_logo.gif http://www.nature.com/nsmb/ A rule of seven in Watson-Crick base-pairing of mismatched sequences http://feeds.nature.com/~r/nsmb/rss/aop/~3/XUvy1L_4_Og/nsmb.2294 Sequence recognition through base pairing is essential for DNA repair and gene regulation, but the basic rules underlying this process have been unclear. Data from single-molecule fluorescence studies, used to visualize annealing and melting reactions of two untethered strands containing a single mismatch, suggest that seven contiguous base pairs are needed for rapid annealing of DNA and RNA. A rule of seven in Watson-Crick base-pairing of mismatched sequences

Nature Structural & Molecular Biology. doi:10.1038/nsmb.2294

Authors: Ibrahim I Cisse, Hajin Kim & Taekjip Ha

]]> A rule of seven in Watson-Crick base-pairing of mismatched sequences Ibrahim I Cisse Hajin Kim Taekjip Ha doi:10.1038/nsmb.2294 Nature Structural & Molecular Biology 2012-05-13 Nature Structural & Molecular Biology 2012-05-13 10.1038/nsmb.2294 http://dx.doi.org/10.1038/nsmb.2294 Article http://dx.doi.org/10.1038/nsmb.2294 A locally closed conformation of a bacterial pentameric proton-gated ion channel http://feeds.nature.com/~r/nsmb/rss/aop/~3/jbpe-JC8_6Y/nsmb.2307 Pentameric ligand-gated ion channels (pLGICs) mediate fast synaptic signaling in response to neurotransmitter binding, but the conformational changes induced by neurotransmitter binding are unknown. The crystal structures of mutated GLIC, a bacterial pLGIC homolog, reveal a novel, locally closed channel conformation that provides insight into pLGIC allosteric transitions. A locally closed conformation of a bacterial pentameric proton-gated ion channel

Nature Structural & Molecular Biology. doi:10.1038/nsmb.2307

Authors: Marie S Prevost, Ludovic Sauguet, Hugues Nury, Catherine Van Renterghem, Christèle Huon, Frederic Poitevin, Marc Baaden, Marc Delarue & Pierre-Jean Corringer

]]> A locally closed conformation of a bacterial pentameric proton-gated ion channel Marie S Prevost Ludovic Sauguet Hugues Nury Catherine Van Renterghem Christèle Huon Frederic Poitevin Marc Baaden Marc Delarue Pierre-Jean Corringer doi:10.1038/nsmb.2307 Nature Structural & Molecular Biology 2012-05-13 Nature Structural & Molecular Biology 2012-05-13 10.1038/nsmb.2307 http://dx.doi.org/10.1038/nsmb.2307 Article http://dx.doi.org/10.1038/nsmb.2307 Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine http://feeds.nature.com/~r/nsmb/rss/aop/~3/pEuSSzSUfN0/nsmb.2288 A biochemical study reveals the AAA+ protein unfoldase ClpX functions as a closed ring and identifies regions required for intersubunit coupling during the ATPase cycle. These findings provide important insights on the ClpX mechanism that may be extended to other AAA+ proteins. Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine

Nature Structural & Molecular Biology. doi:10.1038/nsmb.2288

Authors: Steven E Glynn, Andrew R Nager, Tania A Baker & Robert T Sauer

]]> Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine Steven E Glynn Andrew R Nager Tania A Baker Robert T Sauer doi:10.1038/nsmb.2288 Nature Structural & Molecular Biology 2012-05-06 Nature Structural & Molecular Biology 2012-05-06 10.1038/nsmb.2288 http://dx.doi.org/10.1038/nsmb.2288 Article http://dx.doi.org/10.1038/nsmb.2288 A glutamate switch controls voltage-sensitive phosphatase function http://feeds.nature.com/~r/nsmb/rss/aop/~3/36XQkGxRxCE/nsmb.2289 The voltage-sensing domain of Ci-VSP regulates the enzymatic activity of its PTEN-like phosphatase domain. New structural and functional data identify a gating loop that controls access to the enzyme's active site and is coupled to voltage sensor movements. A glutamate switch controls voltage-sensitive phosphatase function

Nature Structural & Molecular Biology. doi:10.1038/nsmb.2289

Authors: Lijun Liu, Susy C Kohout, Qiang Xu, Simone Müller, Christopher R Kimberlin, Ehud Y Isacoff & Daniel L Minor

]]> A glutamate switch controls voltage-sensitive phosphatase function Lijun Liu Susy C Kohout Qiang Xu Simone Müller Christopher R Kimberlin Ehud Y Isacoff Daniel L Minor doi:10.1038/nsmb.2289 Nature Structural & Molecular Biology 2012-05-06 Nature Structural & Molecular Biology 2012-05-06 10.1038/nsmb.2289 http://dx.doi.org/10.1038/nsmb.2289 Article http://dx.doi.org/10.1038/nsmb.2289 Real-time assembly landscape of bacterial 30S translation initiation complex http://feeds.nature.com/~r/nsmb/rss/aop/~3/40lA__EmDBo/nsmb.2285 Translation initiation proceeds in several steps, and one of the early events involves the binding of three initiation factors, mRNA and initiator tRNA to the 30S ribosomal subunit, which is known as the 30S pre-initiation complex (PIC) assembly. Systematic FRET studies now uncover the kinetically favored assembly pathway of the 30S PIC. Real-time assembly landscape of bacterial 30S translation initiation complex

Nature Structural & Molecular Biology. doi:10.1038/nsmb.2285

Authors: Pohl Milón, Cristina Maracci, Liudmila Filonava, Claudio O Gualerzi & Marina V Rodnina

]]> Real-time assembly landscape of bacterial 30S translation initiation complex Pohl Milón Cristina Maracci Liudmila Filonava Claudio O Gualerzi Marina V Rodnina doi:10.1038/nsmb.2285 Nature Structural & Molecular Biology 2012-05-06 Nature Structural & Molecular Biology 2012-05-06 10.1038/nsmb.2285 http://dx.doi.org/10.1038/nsmb.2285 Article http://dx.doi.org/10.1038/nsmb.2285 Structural basis for cisplatin DNA damage tolerance by human polymerase η during cancer chemotherapy http://feeds.nature.com/~r/nsmb/rss/aop/~3/wZKtWtn5e-0/nsmb.2295 Cisplatin forms intrastrand cross-links on DNA and is a widely used chemotherapy agent. Among human translesion DNA polymerases, Pol-η can bypass cisplatin adducts. The crystal structure of human Pol-η in complex with a DNA template with a cisplatin lesion is now presented. In addition to the larger active site, the structure reveals specific interactions with the adduct by residues that are not conserved in other translesion polymerases. Structural basis for cisplatin DNA damage tolerance by human polymerase η during cancer chemotherapy

Nature Structural & Molecular Biology. doi:10.1038/nsmb.2295

Authors: Ajay Ummat, Olga Rechkoblit, Rinku Jain, Jayati Roy Choudhury, Robert E Johnson, Timothy D Silverstein, Angeliki Buku, Samer Lone, Louise Prakash, Satya Prakash & Aneel K Aggarwal

]]> Structural basis for cisplatin DNA damage tolerance by human polymerase η during cancer chemotherapy Ajay Ummat Olga Rechkoblit Rinku Jain Jayati Roy Choudhury Robert E Johnson Timothy D Silverstein Angeliki Buku Samer Lone Louise Prakash Satya Prakash Aneel K Aggarwal doi:10.1038/nsmb.2295 Nature Structural & Molecular Biology 2012-05-06 Nature Structural & Molecular Biology 2012-05-06 10.1038/nsmb.2295 http://dx.doi.org/10.1038/nsmb.2295 Article http://dx.doi.org/10.1038/nsmb.2295 Efficiency and specificity in microRNA biogenesis http://feeds.nature.com/~r/nsmb/rss/aop/~3/V45N4RA9shI/nsmb.2293 Primary microRNA cleavage by the Microprocessor complex comprising Drosha and DGCR8 needs to be specific yet efficient. Mathematical modeling complemented with experimental analysis now shows that autoregulatory feedback on DGCR8 expression is crucial for balancing the efficiency and specificity of Microprocessor activity. Efficiency and specificity in microRNA biogenesis

Nature Structural & Molecular Biology. doi:10.1038/nsmb.2293

Authors: Omer Barad, Mati Mann, Elik Chapnik, Archana Shenoy, Robert Blelloch, Naama Barkai & Eran Hornstein

Primary microRNA cleavage by the Drosha–Dgcr8 'Microprocessor' complex is critical for microRNA biogenesis. Yet, the Microprocessor may also cleave other nuclear RNAs in a nonspecific manner. We studied Microprocessor function using mathematical modeling and experiments in mouse and human tissues. We found that the autoregulatory feedback on Microprocessor expression is instrumental for balancing the efficiency and specificity of its activity by effectively tuning Microprocessor levels to those of its pri-miRNA substrate.

]]> Efficiency and specificity in microRNA biogenesis Omer Barad Mati Mann Elik Chapnik Archana Shenoy Robert Blelloch Naama Barkai Eran Hornstein doi:10.1038/nsmb.2293 Nature Structural & Molecular Biology 2012-05-13 Nature Structural & Molecular Biology 2012-05-13 10.1038/nsmb.2293 http://dx.doi.org/10.1038/nsmb.2293 Brief Communication http://dx.doi.org/10.1038/nsmb.2293