IDENTIFICATION OF AN MESSENGER-RNA ELEMENT PROMOTING RATE-LIMITING CLEAVAGE OF THE POLYCISTRONIC PUF MESSENGER-RNA IN RHODOBACTER-CAPSULATUS BY AN ENZYME SIMILAR TO RNASE-E

IDENTIFICATION OF AN MESSENGER-RNA ELEMENT PROMOTING RATE-LIMITING CLEAVAGE OF THE POLYCISTRONIC PUF MESSENGER-RNA IN RHODOBACTER-CAPSULATUS BY AN ENZYME SIMILAR TO RNASE-E
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DOI:
10.1111/j.1365-2958.1995.tb02277.x
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发表时间:
1995-03-01
影响因子:
3.6
通讯作者:
KLUG, G
KLUG, G
中科院分区:
生物学2区
文献类型:
--
作者:
FRITSCH, J;ROTHFUCHS, R;KLUG, G

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我们已经确定了一个mRNA元件,参与了最初的裂解的pufBALMX mRNA物种在红细菌荚膜。该核糖核酸内切酶识别位点是第一个在大肠杆菌以外的细菌物种中鉴定的,与大肠杆菌中被核糖核酸内切酶E切割的mRNA序列具有很强的相似性。杆菌在R. capsulatus的体外裂解进一步支持E. coli中转录本。capsulatus提取物的位点归因于RNase E和来自R. capsulatus与抗E. coli RNase E.我们的数据提供的证据表明,mRNA降解在不同的细菌物种的酶具有相似的识别序列和活动。我们提出了一个模型,属性的多顺反子PUF转录的稳定性的片段差异的mRNA衰变促进和mRNA衰变阻碍元素的特定分布。
We have identified an mRNA element that is involved in the initial cleavage of the pufBALMX mRNA species in Rhodobacter capsulatus. This endoribonuclease recognition site, the first to be identified in a bacterial species other than Escherichia coli, shows strong similarities to mRNA sequences cleaved by the endoribonuclease E in E. coli. The presence of an RNase E-like enzyme in R. capsulatus is further supported by in vitro cleavage of E. coli transcripts by R. capsulatus extracts at sites attributed to RNase E and by the cross-reaction of a polypeptide from R. capsulatus with antisera against E. coli RNase E. Our data provide evidence that mRNAs are degraded in different bacterial species by enzymes with similar recognition sequences and activities. We present a model that attributes the segmental differences in stability of the polycistronic puf transcript to a specific distribution of mRNA decay-promoting and mRNA decay-impeding elements.