Identification and functional analysis of Relish homologs in the silkworm, Bombyx mori.

Identification and functional analysis of Relish homologs in the silkworm, Bombyx mori. Research Abstract Details 

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Identification and functional analysis of Relish homologs in the silkworm, Bombyx mori. Abstract Text:

Hiromitsu Tanaka,Hiroyuki Matsuki,Seiichi Furukawa,Aki Sagisaka,Eiji Kotani,Hajime Mori,Minoru Yamakawa,

Two cDNAs designated BmRelish1 and 2, that encode Relish homologs, were cloned from the silkworm, Bombyx mori. BmRelish1 had an IkappaB-like domain with 5 ankyrin repeats in addition to Rel homology domain (RHD), nuclear localization signal (NLS), and acidic and hydrophobic amino acids (AHAA) rich regions. On the other hand, BmRelish2 lacked the AHAA and ankyrin repeats (ANK). Knockdown of the BmRelish gene in transgenic silkworms resulted in failure of the activation of antimicrobial peptide genes by Escherichia coli, suggesting that BmRelish plays an important role in antimicrobial peptide gene expression. Functional analysis of BmRelish1 and 2 in mbn-2 cells showed that both Relish homologs do not activate promoters of B. mori antimicrobial peptide genes encoding cecropin B1, attacin, lebocin 3 and lebocin 4. However, a gene construct BmRelish1-d2 lacking the ANK strongly activated promoters of these genes. Another gene construct lacking AHAA and ANK failed to activate these genes, suggesting that BmRelish becomes active by removal of the ANK and that the AHAA-rich region is a transactivation domain. BmRelish2 was shown to repress activation of Cecropin B1 gene expression by BmRelish1-d2, suggesting that BmRelish2 plays a role as a dominant negative factor against the BmRelish1 active form. Necessity of kappaB sites of Cecropin B1, Attacin and Lebocin 4 genes for the full activation of these genes by BmRelish1-d2 was confirmed. The requirement of the mandatory kappaB sites for Lebocin 4 gene expression was different between BmRelish1 active form and BmRelA, suggesting differential roles for kappaB sites in antimicrobial peptide gene activation by different transcription factors. The binding of the RHD portion of BmRelish1 fusion protein to the kappaB sites of Cecropin B1 and Attacin genes was also confirmed.

Identification and functional analysis of Relish homologs in the silkworm, Bombyx mori. Publishing Authors By Initials

H Tanaka,H Matsuki,S Furukawa,A Sagisaka,E Kotani,H Mori,M Yamakawa,

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

PUBMED ID PMID:

MEDLINE DATE: 2007 Sep-Oct

Identification and functional analysis of Relish homologs in the silkworm, Bombyx mori. Journal Published:

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

Journal: Biochimica et biophysica acta

VOLUME: 1769

Page Numbers: 559-68

Journal Abbreviation: Biochim. Biophys. Acta

ISSN: 0006-3002

DAY: 19

MONTH: 07

YEAR: 2007

Identification and functional analysis of Relish homologs in the silkworm, Bombyx mori. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 217513

Identification and functional analysis of Relish homologs in the silkworm, Bombyx mori. Keywords Mesh Terms:

KEYWORDS: Transcription Factors

MESH TERMS: metabolism

Chemical & Substance for Abstract: Identification and functional analysis of Relish homologs in the silkworm, Bombyx mori. Information

Substance Name: lebocin protein, Bombyx mori

Registry Number: 0

Grant and Affiliation Information for Identification and functional analysis of Relish homologs in the silkworm, Bombyx mori.

AFFILIATION: Innate Immunity Research Unit, National Institute of Agrobiological Sciences, Owashi 1-2, Tsukuba, Ibaraki 305-8634, Japan.

Country: Netherlands

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MEDLINETA: Biochim Biophys Acta

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