Nature Structural & Molecular Biology An integrated forum for structural and molecular studies. http://www.nature.com/nsmb/current_issue/ Nature Publishing Group en © 2008 Nature Publishing Group Nature Structural & Molecular Biology 1545-9993 1545-9985 © 2008 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/ Mechanics of membrane fusion http://dx.doi.org/10.1038/nsmb.1455 Mechanics of membrane fusion

Nature Structural & Molecular Biology 15, 675 (2008). doi:10.1038/nsmb.1455

Authors: Leonid V Chernomordik & Michael M Kozlov

]]> Mechanics of membrane fusion Leonid V Chernomordik Michael M Kozlov doi:10.1038/nsmb.1455 Nature Structural & Molecular Biology 15, 675 (2008) 2008-07-03 Nature Structural & Molecular Biology 2008-07-03 15 7 Review 675 683 Viral membrane fusion http://dx.doi.org/10.1038/nsmb.1456 Viral membrane fusion

Nature Structural & Molecular Biology 15, 690 (2008). doi:10.1038/nsmb.1456

Author: Stephen C Harrison

]]> Viral membrane fusion Stephen C Harrison doi:10.1038/nsmb.1456 Nature Structural & Molecular Biology 15, 690 (2008) 2008-07-03 Nature Structural & Molecular Biology 2008-07-03 15 7 Review 690 698 The fusion pores of Ca2+-triggered exocytosis http://dx.doi.org/10.1038/nsmb.1449 The fusion pores of Ca2+-triggered exocytosis

Nature Structural & Molecular Biology 15, 684 (2008). doi:10.1038/nsmb.1449

Authors: Meyer B Jackson & Edwin R Chapman

]]> The fusion pores of Ca2+-triggered exocytosis Meyer B Jackson Edwin R Chapman doi:10.1038/nsmb.1449 Nature Structural & Molecular Biology 15, 684 (2008) 2008-07-03 Nature Structural & Molecular Biology 2008-07-03 15 7 Review 684 689 Synaptic vesicle fusion http://dx.doi.org/10.1038/nsmb.1450 Synaptic vesicle fusion

Nature Structural & Molecular Biology 15, 665 (2008). doi:10.1038/nsmb.1450

Authors: Josep Rizo & Christian Rosenmund

]]> Synaptic vesicle fusion Josep Rizo Christian Rosenmund doi:10.1038/nsmb.1450 Nature Structural & Molecular Biology 15, 665 (2008) 2008-07-03 Nature Structural & Molecular Biology 2008-07-03 15 7 Review 665 674 Membrane fusion http://dx.doi.org/10.1038/nsmb.1451 Membrane fusion

Nature Structural & Molecular Biology 15, 658 (2008). doi:10.1038/nsmb.1451

Authors: William Wickner & Randy Schekman

]]> Membrane fusion William Wickner Randy Schekman doi:10.1038/nsmb.1451 Nature Structural & Molecular Biology 15, 658 (2008) 2008-07-03 Nature Structural & Molecular Biology 2008-07-03 15 7 Review 658 664 Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT http://dx.doi.org/10.1038/nsmb.1436 Group II chaperonins, such as TriC/CCT, have a build-in lid that can cover the folding chamber and functions in an analogous way to the GroES-like proteins used by their Group I counterparts. Structural and modeling data suggest an allosteric mechanism of TriC lid closure that differs from GroES–GroEL systems. Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT

Nature Structural & Molecular Biology 15, 746 (2008). doi:10.1038/nsmb.1436

Authors: Christopher R Booth, Anne S Meyer, Yao Cong, Maya Topf, Andrej Sali, Steven J Ludtke, Wah Chiu & Judith Frydman

]]> Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT Christopher R Booth Anne S Meyer Yao Cong Maya Topf Andrej Sali Steven J Ludtke Wah Chiu Judith Frydman doi:10.1038/nsmb.1436 Nature Structural & Molecular Biology 15, 746 (2008) 2008-06-08 Nature Structural & Molecular Biology 2008-06-08 15 7 Article 746 753 Capped small RNAs and MOV10 in human hepatitis delta virus replication http://dx.doi.org/10.1038/nsmb.1440 Both genomic and antigenomic hepatitis delta virus (HDV) RNAs have hairpin-shaped ends. Small capped RNAs have now been identified from both genomic and antigenomic RNAs, and the human homolog of the Arabidopsis RNA amplification factor (SDE3) has been implicated in the replication of HDV. Capped small RNAs and MOV10 in human hepatitis delta virus replication

Nature Structural & Molecular Biology 15, 714 (2008). doi:10.1038/nsmb.1440

Authors: Dirk Haussecker, Dan Cao, Yong Huang, Poornima Parameswaran, Andrew Z Fire & Mark A Kay

]]> Capped small RNAs and MOV10 in human hepatitis delta virus replication Dirk Haussecker Dan Cao Yong Huang Poornima Parameswaran Andrew Z Fire Mark A Kay doi:10.1038/nsmb.1440 Nature Structural & Molecular Biology 15, 714 (2008) 2008-06-15 Nature Structural & Molecular Biology 2008-06-15 15 7 Article 714 721 Molecular mechanism of energy conservation in polysulfide respiration http://dx.doi.org/10.1038/nsmb.1434 Polysulfides are chains of sulfur atoms abundant in extreme environments. Some organisms reduce polysulfides, and this reaction may be coupled to respiratory processes. Now the structure of the multicomponent membrane complex that catalyzes this reaction is solved, revealing a potential proton channel that could have a role in energy conservation. Molecular mechanism of energy conservation in polysulfide respiration

Nature Structural & Molecular Biology 15, 730 (2008). doi:10.1038/nsmb.1434

Authors: Mika Jormakka, Ken Yokoyama, Takahiro Yano, Masatada Tamakoshi, Satoru Akimoto, Tatsuro Shimamura, Paul Curmi & So Iwata

]]> Molecular mechanism of energy conservation in polysulfide respiration Mika Jormakka Ken Yokoyama Takahiro Yano Masatada Tamakoshi Satoru Akimoto Tatsuro Shimamura Paul Curmi So Iwata doi:10.1038/nsmb.1434 Nature Structural & Molecular Biology 15, 730 (2008) 2008-06-08 Nature Structural & Molecular Biology 2008-06-08 15 7 Article 730 737 Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion http://dx.doi.org/10.1038/nsmb.1433 The cooperative action of multiple trans SNARE complexes are a likely requirement for successful membrane fusion. New in vitro analyses reveal the kinetic timescales of the sequential steps of the fusion process, beginning with trans SNARE pairing and clustering of vesicle SNARE proteins, proceeding to hemifusion of outer bilayer leaflets, and ending with full fusion. Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion

Nature Structural & Molecular Biology 15, 700 (2008). doi:10.1038/nsmb.1433

Authors: Xiaobing Lu, Yinghui Zhang & Yeon-Kyun Shin

]]> Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion Xiaobing Lu Yinghui Zhang Yeon-Kyun Shin doi:10.1038/nsmb.1433 Nature Structural & Molecular Biology 15, 700 (2008) 2008-06-15 Nature Structural & Molecular Biology 2008-06-15 15 7 Article 700 706 Asymmetric bidirectional replication at the human DBF4 origin http://dx.doi.org/10.1038/nsmb.1439 The origin of replication located at the human DBF4 promoter is finely characterized. Two initiation zones are on opposite strands and 400 bp apart, being fired in a sequential way, in a manner similar to replication at bacterial oriC. Asymmetric bidirectional replication at the human DBF4 origin

Nature Structural & Molecular Biology 15, 722 (2008). doi:10.1038/nsmb.1439

Authors: Julia Romero & Hoyun Lee

]]> Asymmetric bidirectional replication at the human DBF4 origin Julia Romero Hoyun Lee doi:10.1038/nsmb.1439 Nature Structural & Molecular Biology 15, 722 (2008) 2008-06-08 Nature Structural & Molecular Biology 2008-06-08 15 7 Article 722 729 Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP http://dx.doi.org/10.1038/nsmb.1448 Rtt109 is a relatively recently identified yeast histone acetyltransferase that forms distinct complexes with two histone chaperones. The structure of Rtt109 now reveals that while functionally distinct, it is structurally homologous to mammalian p300/CBP, which previously appeared to not contain a counterpart in yeast. Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP

Nature Structural & Molecular Biology 15, 738 (2008). doi:10.1038/nsmb.1448

Authors: Yong Tang, Marc A Holbert, Hugo Wurtele, Katrina Meeth, Walter Rocha, Marlene Gharib, Eva Jiang, Pierre Thibault, Alain Verrault, Philip A Cole & Ronen Marmorstein

]]> Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP Yong Tang Marc A Holbert Hugo Wurtele Katrina Meeth Walter Rocha Marlene Gharib Eva Jiang Pierre Thibault Alain Verrault Philip A Cole Ronen Marmorstein doi:10.1038/nsmb.1448 Nature Structural & Molecular Biology 15, 738 (2008) 2008-06-22 Nature Structural & Molecular Biology 2008-06-22 15 7 Article 738 745 Complexin and Ca2+ stimulate SNARE-mediated membrane fusion http://dx.doi.org/10.1038/nsmb.1446 Complexin is one of several regulatory molecules known to be important for SNARE-mediated fusion that occurs during neurotransmitter release. In vitro data now suggest that complexin plays inhibitory and Ca2+- dependent stimulatory roles that may be correlated to changing interactions with the SNARE complex. Complexin and Ca2+ stimulate SNARE-mediated membrane fusion

Nature Structural & Molecular Biology 15, 707 (2008). doi:10.1038/nsmb.1446

Authors: Tae-Young Yoon, Xiaobing Lu, Jiajie Diao, Soo-Min Lee, Taekjip Ha & Yeon-Kyun Shin

]]> Complexin and Ca2+ stimulate SNARE-mediated membrane fusion Tae-Young Yoon Xiaobing Lu Jiajie Diao Soo-Min Lee Taekjip Ha Yeon-Kyun Shin doi:10.1038/nsmb.1446 Nature Structural & Molecular Biology 15, 707 (2008) 2008-06-15 Nature Structural & Molecular Biology 2008-06-15 15 7 Article 707 713 Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation http://dx.doi.org/10.1038/nsmb.1443 Cytoplasmic O-GlcNac modification of proteins is thought to have dynamic interplay with phosphorylation and thus be involved in regulation of signaling processes. The complete structure of an OGT homolog is now presented, suggesting how diverse ligands can be presented to the active site of the enzyme. Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation

Nature Structural & Molecular Biology 15, 764 (2008). doi:10.1038/nsmb.1443

Authors: Carlos Martinez-Fleites, Matthew S Macauley, Yuan He, David L Shen, David J Vocadlo & Gideon J Davies

N-Acetylglucosamine (O-GlcNAc) modification of proteins provides a mechanism for the control of diverse cellular processes through a dynamic interplay with phosphorylation. UDP-GlcNAc:polypeptidyl transferase (OGT) catalyzes O-GlcNAc addition. The structure of an intact OGT homolog and kinetic analysis of human OGT variants reveal a contiguous superhelical groove that directs substrates to the active site.

]]> Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation Carlos Martinez-Fleites Matthew S Macauley Yuan He David L Shen David J Vocadlo Gideon J Davies doi:10.1038/nsmb.1443 Nature Structural & Molecular Biology 15, 764 (2008) 2008-06-08 Nature Structural & Molecular Biology 2008-06-08 15 7 Brief Communication 764 765 A second binding site for double-stranded RNA in TLR3 and consequences for interferon activation http://dx.doi.org/10.1038/nsmb.1453 Toll-like receptor 3 (TLR3) recognizes double-stranded RNA (dsRNA) molecules produced by many viruses and activates an inflammatory response. Synthetic dsRNAs such as small interfering RNAs have been shown to activate TLR3. Now the TLR3 ectodomain is found to contain two dsRNA binding sites, and the implications for dsRNA recognition and selectivity and downstream signaling are discussed. A second binding site for double-stranded RNA in TLR3 and consequences for interferon activation

Nature Structural & Molecular Biology 15, 761 (2008). doi:10.1038/nsmb.1453

Authors: Nina Pirher, Karolina Ivičak, Jelka Pohar, Mojca Benčina & Roman Jerala

]]> A second binding site for double-stranded RNA in TLR3 and consequences for interferon activation Nina Pirher Karolina Ivičak Jelka Pohar Mojca Benčina Roman Jerala doi:10.1038/nsmb.1453 Nature Structural & Molecular Biology 15, 761 (2008) 2008-06-22 Nature Structural & Molecular Biology 2008-06-22 15 7 Brief Communication 761 763 Some classic papers in the field of membrane fusion—a personal view http://dx.doi.org/10.1038/nsmb0708-655 Every field of research has influential papers that have shaped and guided future work. Reinhard Jahn gives his picks for membrane fusion and a little bit of history about how the field has developed. Some classic papers in the field of membrane fusion—a personal view

Nature Structural & Molecular Biology 15, 655 (2008). doi:10.1038/nsmb0708-655

Author: Reinhard Jahn

Every field of research has influential papers that have shaped and guided future work. Reinhard Jahn gives his picks for membrane fusion and a little bit of history about how the field has developed.

]]> Some classic papers in the field of membrane fusion—a personal view Reinhard Jahn doi:10.1038/nsmb0708-655 Nature Structural & Molecular Biology 15, 655 (2008) Nature Structural & Molecular Biology 15 7 Essay 655 657 GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore http://dx.doi.org/10.1038/nsmb.1442 The protective antigen (PA) moiety of anthrax toxin exists as a stable prepore, converting into the pore form under low pH to translocate the enzymatic components across the host cell membrane. The PA pore rapidly aggregates in solution, and it is now shown that the chaperone GroEL can stabilize the PA pore, allowing single-particle EM analysis. This method could be useful for other membrane protein complexes. GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore

Nature Structural & Molecular Biology 15, 754 (2008). doi:10.1038/nsmb.1442

Authors: Hiroo Katayama, Blythe E Janowiak, Marek Brzozowski, Jordan Juryck, Scott Falke, Edward P Gogol, R John Collier & Mark T Fisher

]]> GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore Hiroo Katayama Blythe E Janowiak Marek Brzozowski Jordan Juryck Scott Falke Edward P Gogol R John Collier Mark T Fisher doi:10.1038/nsmb.1442 Nature Structural & Molecular Biology 15, 754 (2008) 2008-06-22 Nature Structural & Molecular Biology 2008-06-22 15 7 Technical Report 754 760 Bringing it together http://dx.doi.org/10.1038/nsmb0708-653 An in-depth look at membrane fusion—a process essential for communication within and between cells—is presented in this issue of Nature Structural & Molecular Biology. Bringing it together

Nature Structural & Molecular Biology 15, 653 (2008). doi:10.1038/nsmb0708-653

An in-depth look at membrane fusion—a process essential for communication within and between cells—is presented in this issue of Nature Structural & Molecular Biology.

]]> Bringing it together doi:10.1038/nsmb0708-653 Nature Structural & Molecular Biology 15, 653 (2008) Nature Structural & Molecular Biology 15 7 Editorial 653 653 Research highlights http://dx.doi.org/10.1038/nsmb0708-699 Research highlights

Nature Structural & Molecular Biology 15, 699 (2008). doi:10.1038/nsmb0708-699

]]> Research highlights doi:10.1038/nsmb0708-699 Nature Structural & Molecular Biology 15, 699 (2008) Nature Structural & Molecular Biology 15 7 Research Highlights 699 699