Shi's team, Cells, analyzes yeast ILS state clippings

In the early hours of September 15th, Beijing time, Cell published a paper entitled "
" by Professor Shi's team online, which analyzed the intrinsic zirtosis ILS complex with an average resolution of 3.5A for brewing yeast. Professor Shi Yigong is the author of this article, signed by West Lake University, Zhejiang West Lake Institute of Advanced Studies, Tsinghua University School of Life Ph.D. Wan Yu Xue, Gao Jingxing Center of Excellence Scholar Yan Entrepreneurship Ph.D., Ph.D. student Bai Wei is the co-first author of this article.
of the inclusions is mainly achieved through a two-step transester reaction, which is catalyzed by the shear body (Figure a below). For each inclusion, in order to regulate the reaction of the various substumps at the appropriate time to present the appropriate composition to play its activity, the shear body components in a highly accurate sequence of binding and dissociate, assembled into a series of molecular machines with different compositions, collectively known as shears. Depending on their bio-chemical properties during RNA scissors, these shears are divided into several states, such as E, A, B, Bact, B, C, C, P, ILS , etc. (Figure b below).from: Shi, Y. (2017). The Spliceosome: A Protein-Directed Metalloribozyme. Journal of Molecular Biology, 429(17), 2640-2653.
in this structure, for the first time, four key eggs involved in the shear disintegration and a shear factor that played an important role in the shear disintegration process were observed. The analysis of the structure complements the key information of mRNA shearing post-shear disintegration, describes the change of the catalytic reaction activity center after the shear completes the transester reaction and is about to disintegrate, and proposes two molecular models of possible shear disintegrate from the perspective of structural biology. The analysis of this structure provides an important basis for speculation on the structure of shear disintegration for many years in the field.
shear is made up of five small RNA proteins (snRNP), nineteen complexes , nineteen complexes, nineteen complex-related proteins (NTC Related) and a range of auxiliary proteins, involving more than 100 proteins and at least five RNA molecules. During the cutting process, the clipper's pre-body messenger RNA molecules are centered, gradually assembled in a highly precise sequence, and large-scale structural recombination occurs, enabling it to perform complex cutting tasks. Scissors are an integral part of normal life activities of the nuclei, so it is of great biological significance to obtain the structure of the various states of the shear in the assembly, activation, and catalytic reaction process is one of the most fundamental and challenging structural biology challenges (In early 2014, Nature published an opinion article reviewing the centennial of crystallology, treating the structure of the shear and nucleosome complex as the most desired protein complex to be parsed in the future).
August 2015, Professor Shi's team has reported on the high-resolution structure of five key state shear complexes in the shear reaction, namely 3.8 E pre-assembled complex tri-snRNP and 3.5 E. Activate state complexBact complex, 3.4 E first catalytic reaction complex after the compound C complex, 4.0 E second step catalytic activation state of C x complex, and 3.6 E containing subsoil shear body ILS complex. The shear state represented by these five high-resolution structures basically covers the key catalytic steps in the entire shear path, provides the most clear structural information in the different working states of the shear to date, and greatly promotes the development of RNA shear research. In May 2017, Professor Shi's team also analyzed the working state of the human-source shear (3.76A second-step catalytic activation of the human-source C-complex), explaining the functional function of the human-source shear catalyzing second-step transester reaction (see BioArt's previous report: Shi's first report on the atomic resolution structure of the human-source shear).
the disintegrating of the
containing the subsoil shear body ILS complex marks the end of the clipping cycle, and as early as August 2015, Professor Shi's team analyzed the internal subsoil shear ils complex of S. pombe 3.6 E. The latest study shows that THELS complex of wine-making yeast and cleavage yeast is highly similar in its overall composition and protein composition, as well as in RNA (below).The ILS complex of brewing yeast instead of cleavage yeast contains three Ntr complex components: ATPase/de-cyclone plp43, Ntr1/Spp382, and Ntr2, in addition to the shearing factor Cwc23. The cleavage yeast contains four proteins: Cwf11, Cwf19, Cwf17, and Cyp1. In addition to Cwf19, the other three proteins do not have a corresponding iso-protein in the brewing yeast.
at the center of the brewing yeast ILS complex, Prp8, Snu114, three 19th complex (NTC) proteins (Cef1, Clf1, Syf2) and 6 NTC-related (The NTR) components (Cwc2, Cwc15, Bud31, Ecm2, Prp45, Prp46) interact with RNA at the active point, and there is a certain similarity between C.complex (see figure below). This structure provides a more reasonable mechanism for understanding the dissocation of ILS complex. (Source: Zhejiang West Lake Institute of Advanced Studies)content reproduced from WeChat public number "
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