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  1. Article ; Online: Non-coding RNA suppresses FUS aggregation caused by mechanistic shear stress on pipetting in a sequence-dependent manner.

    Hamad, Nesreen / Yoneda, Ryoma / So, Masatomo / Kurokawa, Riki / Nagata, Takashi / Katahira, Masato

    Scientific reports

    2021  Volume 11, Issue 1, Page(s) 9523

    Abstract: Fused in sarcoma/translocated in liposarcoma (FUS/TLS) is a multitasking RNA/DNA binding protein. FUS aggregation is implicated in various neurodegenerative diseases. RNA was suggested to modulate phase transition of FUS. Here, we found that FUS ... ...

    Abstract Fused in sarcoma/translocated in liposarcoma (FUS/TLS) is a multitasking RNA/DNA binding protein. FUS aggregation is implicated in various neurodegenerative diseases. RNA was suggested to modulate phase transition of FUS. Here, we found that FUS transforms into the amorphous aggregation state as an instant response to the shear stress caused by usual pipetting even at a low FUS concentration, 100 nM. It was revealed that non-coding RNA can suppress the transformation of FUS into aggregates. The suppressive effect of RNA on FUS aggregation is sequence-dependent. These results suggested that the non-coding RNA could be a prospective suppressor of FUS aggregation caused by mechanistic stress in cells. Our finding might pave the way for more research on the role of RNAs as aggregation inhibitors, which could facilitate the development of therapies for neurodegenerative diseases.
    MeSH term(s) DNA-Binding Proteins/genetics ; Protein Aggregates/genetics ; RNA, Untranslated/genetics ; RNA-Binding Protein FUS/genetics ; RNA-Binding Proteins/genetics ; Shear Strength/physiology
    Chemical Substances DNA-Binding Proteins ; Protein Aggregates ; RNA, Untranslated ; RNA-Binding Protein FUS ; RNA-Binding Proteins
    Language English
    Publishing date 2021-05-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-021-89075-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Direct visualization of the conformational change of FUS/TLS upon binding to promoter-associated non-coding RNA

    Hamad, Nesreen / Watanabe, Hiroki / Uchihashi, Takayuki / Kurokawa, Riki / Nagata, Takashi / Katahira, Masato

    Chemical communications. 2020 Aug. 11, v. 56, no. 64

    2020  

    Abstract: High-speed AFM revealed the conformational change of fused in sarcoma (FUS) from a compact to an extended structure upon binding of non-coding RNA, which is supposed to allow FUS to bind to CBP/p300 for transcriptional interference. Thus, a mechanistic ... ...

    Abstract High-speed AFM revealed the conformational change of fused in sarcoma (FUS) from a compact to an extended structure upon binding of non-coding RNA, which is supposed to allow FUS to bind to CBP/p300 for transcriptional interference. Thus, a mechanistic insight into transcription regulation by FUS and non-coding RNA is provided.
    Keywords non-coding RNA ; sarcoma ; transcription (genetics)
    Language English
    Dates of publication 2020-0811
    Size p. 9134-9137.
    Publishing place The Royal Society of Chemistry
    Document type Article
    Note NAL-AP-2-clean
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d0cc03776a
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Direct visualization of the conformational change of FUS/TLS upon binding to promoter-associated non-coding RNA.

    Hamad, Nesreen / Watanabe, Hiroki / Uchihashi, Takayuki / Kurokawa, Riki / Nagata, Takashi / Katahira, Masato

    Chemical communications (Cambridge, England)

    2020  Volume 56, Issue 64, Page(s) 9134–9137

    Abstract: High-speed AFM revealed the conformational change of fused in sarcoma (FUS) from a compact to an extended structure upon binding of non-coding RNA, which is supposed to allow FUS to bind to CBP/p300 for transcriptional interference. Thus, a mechanistic ... ...

    Abstract High-speed AFM revealed the conformational change of fused in sarcoma (FUS) from a compact to an extended structure upon binding of non-coding RNA, which is supposed to allow FUS to bind to CBP/p300 for transcriptional interference. Thus, a mechanistic insight into transcription regulation by FUS and non-coding RNA is provided.
    MeSH term(s) Green Fluorescent Proteins/chemistry ; Intrinsically Disordered Proteins/chemistry ; Intrinsically Disordered Proteins/metabolism ; Maltose-Binding Proteins/chemistry ; Microscopy, Atomic Force ; Promoter Regions, Genetic ; Protein Binding ; Protein Conformation ; RNA, Untranslated/metabolism ; RNA-Binding Protein FUS/chemistry ; RNA-Binding Protein FUS/metabolism
    Chemical Substances Intrinsically Disordered Proteins ; Maltose-Binding Proteins ; RNA, Untranslated ; RNA-Binding Protein FUS ; Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2020-07-22
    Publishing country England
    Document type Journal Article ; Video-Audio Media
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d0cc03776a
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: RNA sequence and length contribute to RNA-induced conformational change of TLS/FUS.

    Hamad, Nesreen / Mashima, Tsukasa / Yamaoki, Yudai / Kondo, Keiko / Yoneda, Ryoma / Oyoshi, Takanori / Kurokawa, Riki / Nagata, Takashi / Katahira, Masato

    Scientific reports

    2020  Volume 10, Issue 1, Page(s) 2629

    Abstract: Translocated in liposarcoma (TLS)/fused in sarcoma (FUS) is a multitasking DNA/RNA binding protein implicated in cancer and neurodegenerative diseases. Upon DNA damage, TLS is recruited to the upstream region of the cyclin D1 gene (CCND1) through binding ...

    Abstract Translocated in liposarcoma (TLS)/fused in sarcoma (FUS) is a multitasking DNA/RNA binding protein implicated in cancer and neurodegenerative diseases. Upon DNA damage, TLS is recruited to the upstream region of the cyclin D1 gene (CCND1) through binding to the promotor associated non-coding RNA (pncRNA) that is transcribed from and tethered at the upstream region. Binding to pncRNA is hypothesized to cause the conformational change of TLS that enables its inhibitive interaction with histone acetyltransferases and resultant repression of CCND1 expression, although no experimental proof has been obtained. Here, the closed-to-open conformational change of TLS on binding pncRNA was implied by fluorescence resonance energy transfer. A small fragment (31 nucleotides) of the full-length pncRNA (602 nucleotides) was shown to be sufficient for the conformational change of TLS. Dissection of pncRNA identified the G-rich RNA sequence that is critical for the conformational change. The length of RNA was also revealed to be critical for the conformational change. Furthermore, it was demonstrated that the conformational change of TLS is caused by another target DNA and RNA, telomeric DNA and telomeric repeat-containing RNA. The conformational change of TLS on binding target RNA/DNA is suggested to be essential for biological functions.
    MeSH term(s) Base Sequence ; Binding Sites ; Fluorescence Resonance Energy Transfer ; Humans ; Nucleic Acid Conformation ; Promoter Regions, Genetic ; Protein Binding ; Protein Conformation ; RNA, Untranslated/chemistry ; RNA, Untranslated/metabolism ; RNA-Binding Protein FUS/chemistry ; RNA-Binding Protein FUS/metabolism
    Chemical Substances RNA, Untranslated ; RNA-Binding Protein FUS
    Language English
    Publishing date 2020-02-14
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-020-59496-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Accumulation of the FACT complex, as well as histone H3.3, serves as a target marker for somatic hypermutation.

    Aida, Masatoshi / Hamad, Nesreen / Stanlie, Andre / Begum, Nasim A / Honjo, Tasuku

    Proceedings of the National Academy of Sciences of the United States of America

    2013  Volume 110, Issue 19, Page(s) 7784–7789

    Abstract: Somatic hypermutation (SHM) requires not only the expression of activation-induced cytidine deaminase, but also transcription in the target regions. However, how transcription guides activation-induced cytidine deaminase in targeting SHM to the Ig genes ... ...

    Abstract Somatic hypermutation (SHM) requires not only the expression of activation-induced cytidine deaminase, but also transcription in the target regions. However, how transcription guides activation-induced cytidine deaminase in targeting SHM to the Ig genes is not fully understood. Here, we found that the "facilitates chromatin transcription" (FACT) complex promotes SHM by RNAi screening of transcription elongation factors. Furthermore, FACT and histone H3.3, a hallmark of transcription-coupled histone turnover, are enriched at the V(D)J region, 5' flanking sequence of the Sμ switch region and the light chain Jκ 5 segment region in the Ig loci. The regions with the most abundant deposition of FACT and H3.3 were also the most efficient targets of SHM. These results demonstrate the importance of histone-exchanging dynamics at the chromatin of SHM targets, especially in Ig genes.
    MeSH term(s) Cell Line, Tumor ; Chromatin/chemistry ; Chromatin/metabolism ; Cinnamates/metabolism ; Cytidine Deaminase/genetics ; DNA Mutational Analysis ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Genes, Reporter ; Genetic Markers ; Green Fluorescent Proteins/metabolism ; High Mobility Group Proteins/genetics ; High Mobility Group Proteins/metabolism ; Histones/genetics ; Humans ; Hygromycin B/analogs & derivatives ; Hygromycin B/metabolism ; Immunoglobulin Class Switching ; Immunoglobulins/genetics ; RNA Interference ; RNA, Small Interfering/metabolism ; Sequence Analysis, DNA ; Somatic Hypermutation, Immunoglobulin ; Transcription, Genetic ; Transcriptional Elongation Factors/genetics ; Transcriptional Elongation Factors/metabolism
    Chemical Substances Chromatin ; Cinnamates ; DNA-Binding Proteins ; Genetic Markers ; High Mobility Group Proteins ; Histones ; Immunoglobulins ; RNA, Small Interfering ; SSRP1 protein, human ; Transcriptional Elongation Factors ; Green Fluorescent Proteins (147336-22-9) ; Hygromycin B (3XQ2233B0B) ; hygromycin A (3YJY415DDI) ; AICDA (activation-induced cytidine deaminase) (EC 3.5.4.-) ; Cytidine Deaminase (EC 3.5.4.5)
    Language English
    Publishing date 2013-04-22
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1305859110
    Database MEDical Literature Analysis and Retrieval System OnLINE

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