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一种核酸酶，它能特异性切割某些T4信使核糖核酸的核糖体结合位点。

A nuclease that cuts specifically in the ribosome binding site of some T4 mRNAs.

作者信息

Uzan M, Favre R, Brody E

机构信息

Institut de Biologie Physico-Chimique, Paris, France.

出版信息

Proc Natl Acad Sci U S A. 1988 Dec;85(23):8895-9. doi: 10.1073/pnas.85.23.8895.

DOI:10.1073/pnas.85.23.8895
PMID:3057495
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC282613/
Abstract

We have identified a nucleolytic activity in Escherichia coli infected by bacteriophage T4 that introduces cuts in the ribosome binding site of at least two T4 mRNAs. Cutting takes place specifically in the GGAG sequences that are complementary to the 3' end of 16S rRNA (Shine-Dalgarno sequence). The nature of this nucleolytic cut has been investigated by reverse transcriptase mapping, anti-mRNA mapping, utilization of the vaccinia virus guanylyltransferase, and labeling by polynucleotide kinase. We have compared the sequences of target mRNAs with an mRNA of similar sequence but that is not a substrate for the nuclease. This allowed us to narrow down the possibilities for sequence elements that determine nuclease recognition. We hypothesize that this nuclease plays a physiological role in the inhibition of expression of a class of phage proteins.

摘要

我们在被噬菌体T4感染的大肠杆菌中鉴定出一种核酸裂解活性，它能在至少两种T4 mRNA的核糖体结合位点处产生切口。切割专门发生在与16S rRNA 3'端互补的GGAG序列（Shine-Dalgarno序列）中。通过逆转录酶图谱分析、抗mRNA图谱分析、痘苗病毒鸟苷酸转移酶的利用以及多核苷酸激酶标记，对这种核酸裂解切割的性质进行了研究。我们将靶mRNA的序列与具有相似序列但不是核酸酶底物的mRNA进行了比较。这使我们能够缩小决定核酸酶识别的序列元件的可能性范围。我们推测这种核酸酶在抑制一类噬菌体蛋白的表达中发挥生理作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/d22639cc9ccc/pnas00302-0137-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/3667478eae7c/pnas00302-0135-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/aa3734c033d9/pnas00302-0135-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/e167c6797d7a/pnas00302-0136-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/96a777439bd7/pnas00302-0136-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/ac06cfac2c33/pnas00302-0136-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/93bce26bf5ff/pnas00302-0136-d.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/d22639cc9ccc/pnas00302-0137-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/3667478eae7c/pnas00302-0135-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/aa3734c033d9/pnas00302-0135-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/e167c6797d7a/pnas00302-0136-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/96a777439bd7/pnas00302-0136-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/ac06cfac2c33/pnas00302-0136-c.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/93bce26bf5ff/pnas00302-0136-d.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/45c6/282613/d22639cc9ccc/pnas00302-0137-a.jpg

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