Catabolite repression of beta-glucanase synthesis in Bacillus subtilis.

S Krüger, J Stülke, M Hecker
{"title":"Catabolite repression of beta-glucanase synthesis in Bacillus subtilis.","authors":"S Krüger,&nbsp;J Stülke,&nbsp;M Hecker","doi":"10.1099/00221287-139-9-2047","DOIUrl":null,"url":null,"abstract":"<p><p>beta-Glucanase synthesis in Bacillus subtilis was repressed by glucose and other substrates of glycolysis. Experiments with different pts mutants showed that the phosphoenolpyruvate: sugar phosphotransferase system is not involved in carbon catabolite repression of beta-glucanase synthesis. Carbon catabolite repression of beta-glucanase synthesis was completely abolished in a ccpA mutant. An operator structure similar to those upstream of amyE and the xyl operon was found and was shown by site-directed mutagenesis to be the target for carbon catabolite repression of beta-glucanase synthesis. The presence of this operator on a multi-copy plasmid resulted in a reduced repression of both beta-glucanase and alpha-amylase synthesis. It seems likely that the gene encoding these enzymes are part of one regulon with respect to catabolite repression.</p>","PeriodicalId":15884,"journal":{"name":"Journal of general microbiology","volume":"139 9","pages":"2047-54"},"PeriodicalIF":0.0000,"publicationDate":"1993-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1099/00221287-139-9-2047","citationCount":"47","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of general microbiology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1099/00221287-139-9-2047","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 47

Abstract

beta-Glucanase synthesis in Bacillus subtilis was repressed by glucose and other substrates of glycolysis. Experiments with different pts mutants showed that the phosphoenolpyruvate: sugar phosphotransferase system is not involved in carbon catabolite repression of beta-glucanase synthesis. Carbon catabolite repression of beta-glucanase synthesis was completely abolished in a ccpA mutant. An operator structure similar to those upstream of amyE and the xyl operon was found and was shown by site-directed mutagenesis to be the target for carbon catabolite repression of beta-glucanase synthesis. The presence of this operator on a multi-copy plasmid resulted in a reduced repression of both beta-glucanase and alpha-amylase synthesis. It seems likely that the gene encoding these enzymes are part of one regulon with respect to catabolite repression.

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
枯草芽孢杆菌分解代谢抑制β -葡聚糖酶合成。
葡萄糖和其他糖酵解底物抑制枯草芽孢杆菌β -葡聚糖酶的合成。不同突变体的实验表明,磷酸烯醇丙酮酸-糖磷酸转移酶系统不参与碳分解代谢抑制β -葡聚糖酶合成。碳分解代谢物对β -葡聚糖酶合成的抑制作用在ccpA突变体中被完全消除。发现了一个类似于amyE上游和羟基操纵子的操作子结构,并通过位点定向诱变表明它是碳分解代谢物抑制β -葡聚糖酶合成的目标。该操作符在多拷贝质粒上的存在导致β -葡聚糖酶和α -淀粉酶合成的抑制减少。似乎编码这些酶的基因很可能是抑制分解代谢的一个调控的一部分。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Partial protection against genital reinfection by immunization of guinea-pigs with isolated outer-membrane proteins of the chlamydial agent of guinea-pig inclusion conjunctivitis. Calcineurin-dependent growth of an FK506- and CsA-hypersensitive mutant of Saccharomyces cerevisiae. Typing of Clostridium difficile strains by PCR-amplification of variable length 16S-23S rDNA spacer regions. Antimicrobial activity and biosynthesis of indole antibiotics produced by Xenorhabdus nematophilus. Cloning and characterization of a tryptophanase gene from Enterobacter aerogenes SM-18.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1