Cloning of a putative Bombyx mori TFIIB-related factor (BRF).

Cloning of a putative Bombyx mori TFIIB-related factor (BRF).
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假定的家蚕 TFIIB 相关因子 (BRF) 的克隆。

DOI:
10.1002/arch.10120
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发表时间:
2003
期刊:
Archives of insect biochemistry and physiology.
影响因子:
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通讯作者:
Sprague,KarenU
Sprague,KarenU
中科院分区:
--
文献类型:
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作者:
Martinez,MJuanita;Sprague,KarenU

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为了确定负责其保守和专门功能的蛋白质结构域,将来自家蚕(Bombyx mori)的推定 TFIIB 相关因子(BRF)与来自其他生物体的 BRF 进行了比较。 BombyxBRF 编码区由三个独立且重叠的 cDNA 片段组装而成。通过与人BRF1的序列同源性,在家蚕基因组计划“Silkbase”保藏中发现了编码中间部分和3'末端的片段,并且编码N末端的片段是本实验室通过5'RACE方法分离得到的。 Southern 分析表明,家蚕 BRF 是由单拷贝基因编码的。BombyxBRF 包含以下在所有其他 BRF 中都已注意到的结构域,因此很可能提供高度保守的功能:一个锌指结构域、一个不完美重复、三个“BRF 同源”结构域以及 C 末端的一个酸性结构域。正如昆虫和哺乳动物之间的进化关系所预期的那样,BombyxBRF 总体上与果蝇 BRF(55% 相同)比与人类 BRF1(42% 相同)更相似。然而,对各个领域的详细检查揭示了一个显着的例外。与果蝇的结构域 II 相比,家蚕 BRF 的结构域 II 与其人类对应物更相似。这一结果表明,结构域 II 在果蝇中经历了不寻常的分歧,并表明果蝇 BRF 与其他转录因子相互作用的独特模式的结构基础。拱。昆虫生物化学。生理学。 54:55–67, 2003。© 2003 Wiley‐Liss, Inc.
To identify the protein domains responsible for its conserved and specialized functions, putative TFIIB‐Related Factor (BRF) from the silkworm (Bombyx mori)was compared with BRFs from other organisms. TheBombyxBRF coding region was assembled from three separate and overlapping cDNA fragments. Fragments encoding the middle portion and the 3′ end were discovered in theBombyx moriGenome Project “Silkbase” collection through sequence homology with human BRF1, and the fragment encoding the N‐terminus was isolated in our laboratory using the 5′ RACE method. Southern analysis showed that silkworm BRF is encoded by a single‐copy gene.BombyxBRF contains the following domains that have been noted in all other BRFs, and that are likely, therefore, to provide highly conserved functions: a zinc finger domain, an imperfect repeat, three “BRF Homology” domains, and an acidic domain at the C‐terminus. As expected from the evolutionary relationships among insects and mammals,BombyxBRF is more similar overall toDrosophilaBRF (55% identical) than to human BRF1 (42% identical). Detailed examination of individual domains reveals a remarkable exception, however. Domain II ofBombyxBRF is more similar to its human counterpart than toDrosophilaDomain II. This result indicates that Domain II has undergone unusual divergence inDrosophila, and suggests a structural basis forDrosophilaBRF's unique pattern of interaction with other transcription factors. Arch. Insect Biochem. Physiol. 54:55–67, 2003. © 2003 Wiley‐Liss, Inc.