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  1. Article ; Online: Atomic structures of anthrax toxin protective antigen channels bound to partially unfolded lethal and edema factors

    Nathan J. Hardenbrook / Shiheng Liu / Kang Zhou / Koyel Ghosal / Z. Hong Zhou / Bryan A. Krantz

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 10

    Abstract: Abstract Following assembly, the anthrax protective antigen (PA) forms an oligomeric translocon that unfolds and translocates either its lethal factor (LF) or edema factor (EF) into the host cell. Here, we report the cryo-EM structures of heptameric PA ... ...

    Abstract Abstract Following assembly, the anthrax protective antigen (PA) forms an oligomeric translocon that unfolds and translocates either its lethal factor (LF) or edema factor (EF) into the host cell. Here, we report the cryo-EM structures of heptameric PA channels with partially unfolded LF and EF at 4.6 and 3.1-Å resolution, respectively. The first α helix and β strand of LF and EF unfold and dock into a deep amphipathic cleft, called the α clamp, which resides at the interface of two PA monomers. The α-clamp-helix interactions exhibit structural plasticity when comparing the structures of lethal and edema toxins. EF undergoes a largescale conformational rearrangement when forming the complex with the channel. A critical loop in the PA binding interface is displaced for about 4 Å, leading to the weakening of the binding interface prior to translocation. These structures provide key insights into the molecular mechanisms of translocation-coupled protein unfolding and translocation.
    Keywords Science ; Q
    Language English
    Publishing date 2020-02-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article: Membrane association of SadC enhances its diguanylate cyclase activity to control exopolysaccharides synthesis and biofilm formation in Pseudomonas aeruginosa

    Zhu, Bin / Cuilan Liu / Shiheng Liu / Hengjiang Cong / Yihuan Chen / Lichuan Gu / Luyan Z. Ma

    Environmental microbiology. 2016 Oct., v. 18, no. 10

    2016  

    Abstract: Cyclic diguanosine monophosphate (c‐di‐GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a ... ...

    Abstract Cyclic diguanosine monophosphate (c‐di‐GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm. Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c‐di‐GMP in Pseudomonas aeruginosa, an opportunistic pathogen that can cause diverse infections. Here we report the crystal structure of GGDEF domain from SadC and the critical role of the trans‐membrane (TM) domain of SadC with regard to biofilm formation, exopolysaccharide production and motility. We showed that over‐expression of SadC in P. aeruginosa PAO1 totally inhibited swimming motility and significantly enhanced the production of exopolysaccharide Psl. SadC lacking TM domains (SadC₃₀₀–₄₈₇) could not localize on cytoplasmic membrane and form cluster, lost the ability to inhibit the swimming and twitching motility, and showed the attenuated activity to promote Psl production despite that SadC₃₀₀–₄₈₇ was able to catalyze the synthesize of c‐di‐GMP in vitro and in vivo. The GGDEF domain of SadC has a typical GGDEF structure and the α‐helix connected the TM domains with SadC GGDEF domain is essential for SadC to form DGC oligomers. Our data imply that membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers.
    Keywords Pseudomonas aeruginosa ; bacterial motility ; biofilm ; biosynthesis ; cell membranes ; crystal structure ; enzyme activity ; exopolysaccharides ; lifestyle ; plankton ; secondary infection ; swimming
    Language English
    Dates of publication 2016-10
    Size p. 3440-3452.
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note JOURNAL ARTICLE
    ZDB-ID 2020213-1
    ISSN 1462-2920 ; 1462-2912
    ISSN (online) 1462-2920
    ISSN 1462-2912
    DOI 10.1111/1462-2920.13263
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Author Correction

    Xueni Li / Shiheng Liu / Jiansen Jiang / Lingdi Zhang / Sara Espinosa / Ryan C. Hill / Kirk C. Hansen / Z. Hong Zhou / Rui Zhao

    Nature Communications, Vol 9, Iss 1, Pp 1-

    CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into alternative splicing

    2018  Volume 1

    Abstract: The originally published version of this Article contained several errors in Figure 2, panel a: the basepair register in SL3-4 of yeast U1 snRNA was depicted incorrectly; the basepair for A287-U295 in yeast U1 snRNA was erroneously present; basepairs for ...

    Abstract The originally published version of this Article contained several errors in Figure 2, panel a: the basepair register in SL3-4 of yeast U1 snRNA was depicted incorrectly; the basepair for A287-U295 in yeast U1 snRNA was erroneously present; basepairs for U84-G119, G309-U532, A288-U295 and U289-A294 in yeast U1 snRNA were missing; the bulging nucleotide in SL3 of human U1 snRNA was depicted as G instead of C; and the dashed boxes defining the 5′ ss binding site and Sm site in both human and yeast snRNAs were not drawn accurately. These have now been corrected in both the PDF and HTML versions of the Article.
    Keywords Science ; Q
    Language English
    Publishing date 2018-04-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Author Correction

    Xueni Li / Shiheng Liu / Jiansen Jiang / Lingdi Zhang / Sara Espinosa / Ryan C. Hill / Kirk C. Hansen / Z. Hong Zhou / Rui Zhao

    Nature Communications, Vol 9, Iss 1, Pp 1-

    CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into alternative splicing

    2018  Volume 1

    Abstract: The originally published version of this Article contained several errors in Figure 2, panel a: the basepair register in SL3-4 of yeast U1 snRNA was depicted incorrectly; the basepair for A287-U295 in yeast U1 snRNA was erroneously present; basepairs for ...

    Abstract The originally published version of this Article contained several errors in Figure 2, panel a: the basepair register in SL3-4 of yeast U1 snRNA was depicted incorrectly; the basepair for A287-U295 in yeast U1 snRNA was erroneously present; basepairs for U84-G119, G309-U532, A288-U295 and U289-A294 in yeast U1 snRNA were missing; the bulging nucleotide in SL3 of human U1 snRNA was depicted as G instead of C; and the dashed boxes defining the 5′ ss binding site and Sm site in both human and yeast snRNAs were not drawn accurately. These have now been corrected in both the PDF and HTML versions of the Article.
    Keywords Science ; Q
    Language English
    Publishing date 2018-04-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: CryoEM structures of Arabidopsis DDR complexes involved in RNA-directed DNA methylation

    Somsakul Pop Wongpalee / Shiheng Liu / Javier Gallego-Bartolomé / Alexander Leitner / Ruedi Aebersold / Wanlu Liu / Linda Yen / Maria A. Nohales / Peggy Hsuanyu Kuo / Ajay A. Vashisht / James A. Wohlschlegel / Suhua Feng / Steve A. Kay / Z. Hong Zhou / Steven E. Jacobsen

    Nature Communications, Vol 10, Iss 1, Pp 1-

    2019  Volume 12

    Abstract: RNA polymerase V transcription in plants, which is needed DNA methylation and transcriptional silencing, requires components of the DDR complex. Here the authors show that all components of the DDR complex co-localize with Pol V and report the cryoEM ... ...

    Abstract RNA polymerase V transcription in plants, which is needed DNA methylation and transcriptional silencing, requires components of the DDR complex. Here the authors show that all components of the DDR complex co-localize with Pol V and report the cryoEM structures of two complexes associated with Pol V recruitment.
    Keywords Science ; Q
    Language English
    Publishing date 2019-09-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    Inter-library loan at ZB MED

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  6. Article ; Online: CryoEM structures of Arabidopsis DDR complexes involved in RNA-directed DNA methylation

    Somsakul Pop Wongpalee / Shiheng Liu / Javier Gallego-Bartolomé / Alexander Leitner / Ruedi Aebersold / Wanlu Liu / Linda Yen / Maria A. Nohales / Peggy Hsuanyu Kuo / Ajay A. Vashisht / James A. Wohlschlegel / Suhua Feng / Steve A. Kay / Z. Hong Zhou / Steven E. Jacobsen

    Nature Communications, Vol 10, Iss 1, Pp 1-

    2019  Volume 12

    Abstract: RNA polymerase V transcription in plants, which is needed DNA methylation and transcriptional silencing, requires components of the DDR complex. Here the authors show that all components of the DDR complex co-localize with Pol V and report the cryoEM ... ...

    Abstract RNA polymerase V transcription in plants, which is needed DNA methylation and transcriptional silencing, requires components of the DDR complex. Here the authors show that all components of the DDR complex co-localize with Pol V and report the cryoEM structures of two complexes associated with Pol V recruitment.
    Keywords Science ; Q
    Language English
    Publishing date 2019-09-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  7. Article ; Online: CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into alternative splicing

    Xueni Li / Shiheng Liu / Jiansen Jiang / Lingdi Zhang / Sara Espinosa / Ryan C. Hill / Kirk C. Hansen / Z. Hong Zhou / Rui Zhao

    Nature Communications, Vol 8, Iss 1, Pp 1-

    2017  Volume 13

    Abstract: U1 snRNP is critical for 5′ splicing site recognition in pre-mRNA splicing. Here the authors describe the cryo-EM structure of the yeast U1 snRNP and suggest that PrpF39 is an alternative splicing factor essential for the successful recruitment of U1 ... ...

    Abstract U1 snRNP is critical for 5′ splicing site recognition in pre-mRNA splicing. Here the authors describe the cryo-EM structure of the yeast U1 snRNP and suggest that PrpF39 is an alternative splicing factor essential for the successful recruitment of U1 snRNP by other alternative splicing factors.
    Keywords Science ; Q
    Language English
    Publishing date 2017-10-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    Inter-library loan at ZB MED

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  8. Article ; Online: Monomeric ephrinB2 binding induces allosteric changes in Nipah virus G that precede its full activation

    Joyce J. W. Wong / Tracy A. Young / Jiayan Zhang / Shiheng Liu / George P. Leser / Elizabeth A. Komives / Robert A. Lamb / Z. Hong Zhou / Joshua Salafsky / Theodore S. Jardetzky

    Nature Communications, Vol 8, Iss 1, Pp 1-

    2017  Volume 11

    Abstract: Nipah virus causes encephalitis in humans. Here the authors use a multidisciplinary approach to study the binding of the viral attachment protein G to its host receptor ephrinB2 and show that monomeric and dimeric receptors activate distinct ... ...

    Abstract Nipah virus causes encephalitis in humans. Here the authors use a multidisciplinary approach to study the binding of the viral attachment protein G to its host receptor ephrinB2 and show that monomeric and dimeric receptors activate distinct conformational changes in G and discuss implications for receptor-activated virus entry.
    Keywords Science ; Q
    Language English
    Publishing date 2017-10-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    Inter-library loan at ZB MED

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  9. Article ; Online: CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into alternative splicing

    Xueni Li / Shiheng Liu / Jiansen Jiang / Lingdi Zhang / Sara Espinosa / Ryan C. Hill / Kirk C. Hansen / Z. Hong Zhou / Rui Zhao

    Nature Communications, Vol 8, Iss 1, Pp 1-

    2017  Volume 13

    Abstract: U1 snRNP is critical for 5′ splicing site recognition in pre-mRNA splicing. Here the authors describe the cryo-EM structure of the yeast U1 snRNP and suggest that PrpF39 is an alternative splicing factor essential for the successful recruitment of U1 ... ...

    Abstract U1 snRNP is critical for 5′ splicing site recognition in pre-mRNA splicing. Here the authors describe the cryo-EM structure of the yeast U1 snRNP and suggest that PrpF39 is an alternative splicing factor essential for the successful recruitment of U1 snRNP by other alternative splicing factors.
    Keywords Science ; Q
    Language English
    Publishing date 2017-10-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

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