2026-09-24T17:38:41Z https://epublications.vu.lt/oai

oai:vu.lt:elaba:1916546 2026-07-06T19:58:39Z openaireNDLTDDRIVERDART-EUROPE

Endoribonukleazių poveikio ankstyviesiems bakteriofago T4 transkriptams tyrimas /Investigation of the impact of endoribonucleases on bacteriophage T4 early transcripts.Strazdaitė Žielienė, Živilė,info:eu-repo/semantics/openAccessBacteriophage T4 ; RNase G ; RegB ; secondary processing ; PNK.Phage T4 has developed a complex mechanism of ribonucleases control, which needs yet to be investigated. Apart from the impact of endoribonuclease RegB, no other effects of Escherichia coli- or phage-encoded proteins are known to be involved in the degradation of early mRNAs. This study has aimed to identify E. coli endoribonucleases that are involved in secondary processing in RegB-cleaved T4 mRNAs and to determine what phage T4-encoded factors affect the activity of these enzymes. We have shown that the endonucleolytic events at secondary sites of RegB-processed transcripts involve RNases G and E. The RNase G appears to be the main ribonuclease that cleaves all known secondary targets. Moreover, the revealed targets are the first RNase G targets identified in the bacteriophage T4 mRNA. This study has revealed that RNase G can be covalently modified during the infection cycle of bacteriophage T4. However, such modifications do not affect its activity related to the origin of secondary cuts in RegB-processed T4 mRNA. Another important finding is that T4K10 phage encodes defective polynucleotidkinase (PNK). In this study, we have shown that the G14D mutation of phage T4K10 PNK impairs 5'-kinase activity in vivo, as well as in vitro, and leads to the diminished processing of RegB-cleaved transcripts. This study has revealed that both, the T4 RNase RegB- and PNK-mediated activity of the E. coli RNases E and G is designed to accelerate degradation of phage T4 early transcripts.Institutional Repository of Vilnius UniversityTruncaitė, Lidijainfo:eu-repo/semantics/doctoralThesislit2013application/pdfhttps://epublications.vu.lt/object/elaba:1916546/1916546.pdfhttps://repository.vu.lt/VU:ELABAETD1916546&prefLang=en_US