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Bombyx Y-box protein BYB facilitates specific DNA interaction of various DNA binding proteins independently of the cold shock domain.

Bombyx Y-box protein BYB facilitates specific DNA interaction of various DNA binding proteins independently of the cold shock domain. Research Abstract Details 

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  • Bombyx Y-box protein BYB facilitates specific DNA interaction of various DNA binding proteins independently of the cold shock domain. Abstract Text:

    shigeharu takiyaShigeharu Takiya,yoshinori nishitaYoshinori Nishita,susumu ishikawaSusumu Ishikawa,kaoru ohnoKaoru Ohno,taka-aki tamuraTaka-aki Tamura,yoshiaki suzukiYoshiaki Suzuki,

    A new member of the Y-box protein family of the silkworm Bombyx mori (BYB) was co-purified with the fibroin gene enhancer-binding protein FMBP-1, and stimulated the binding of FMBP-1 to its cognate DNA element. However, the stimulatory effect was not specific to FMBP-1, BYB also enhancing the binding of mammalian transcription factors OTF2, SP1 and AP2 to their specific binding elements. Besides the above transcription regulatory factors, BYB facilitated the binding of basal transcription factor TBP, and enhanced transcription from the adenovirus 2 major late promoter in a reconstituted transcription system. Moreover, BYB stimulated the reactions of some restriction endonucleases under cold conditions. The C-terminal region of BYB was sufficient for these stimulatory effects, and the highly conserved cold shock domain (CSD) in the N-terminal region was dispensable. GST-pull down experiments showed that the C-terminal region could interact with DNA independently of the CSD. The above results suggest that the C-terminal region of BYB causes the active interaction of various DNA binding proteins with their targets. Such a function of the C-terminal region of BYB may partly explain the functional diversity of Y-box proteins.

    Bombyx Y-box protein BYB facilitates specific DNA interaction of various DNA binding proteins independently of the cold shock domain. Publishing Authors By Initials

    s takiyaS Takiya,y nishitaY Nishita,s ishikawaS Ishikawa,k ohnoK Ohno,ta tamuraTA Tamura,y suzukiY Suzuki,

    For similar proteins: transcription factors research abstracts see: proteins: transcription factors research

    PUBMED ID PMID:

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    Bombyx Y-box protein BYB facilitates specific DNA interaction of various DNA binding proteins independently of the cold shock domain. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 135

    Page Numbers: 683-93

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Jun

    YEAR: 2004

    Bombyx Y-box protein BYB facilitates specific DNA interaction of various DNA binding proteins independently of the cold shock domain. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Bombyx Y-box protein BYB facilitates specific DNA interaction of various DNA binding proteins independently of the cold shock domain. Keywords Mesh Terms:

    KEYWORDS: Transcription Factors

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Bombyx Y-box protein BYB facilitates specific DNA interaction of various DNA binding proteins independently of the cold shock domain. Information

    Substance Name: DNA

    Registry Number: 9007-49-2

    Grant and Affiliation Information for Bombyx Y-box protein BYB facilitates specific DNA interaction of various DNA binding proteins independently of the cold shock domain.

    AFFILIATION: Laboratory of Gene Function and Regulation, CAST, Hokkaido University, North 10, West 8, Kita-ku, Sapporo 060-0810, Japan. takiya@rmg.hokudai.ac.jp

    Country: Japan

    Japan Research PublicationJapan Research Publication

    AGENCY:

    GRANT:

    ACRONYM:

    MEDLINETA: J Biochem

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER: AB098537

    Number Hits: 0

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