Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:6.5.1.2 (DNA ligase)
 2,749 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The chromosome of the bacterial virus, BA14, a member of the T7 lytic coliphage group, was characterized by direct measurement of its length and construction of a restriction map. The chromosome (39.6 kb) is essentially the same size as T7 (39.9 kb), is devoid of a large number of restriction sites expected for a DNA of this size, and moreover, lacks modification sites for the Escherichia coli Dam and Dcm methyltransferases. The BA14 early region was assigned by testing the ability of specific chromosomal restriction fragments to direct RNA synthesis by E. coli RNA polymerase, and analysis of in vitro RNase III cleavage products of the transcripts. The data support and extend the previous assertion that BA14 is a representative of a distinct T7 subgroup, and limited nucleotide sequence analysis of the BA14 DNA ligase-encoding gene suggests a closer relationship of BA14 to T7 than to T3 phage, another member of the T7 group.
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PMID:Physical map and genetic early region of the T7-related coliphage, BA14. 201 14

The nucleotide sequence through the transcription termination site for Escherichia coli RNA polymerase at the end of the early region of T7 DNA has been determined. RNA chains terminate at adjacent residues in the DNA sequence: about 2/3 of the chains end in C and 1/3 in G. A potential stem and loop structure, containing a stem of eight uninterrupted base pairs and a four-base loop, is centered 17-18 bases ahead of the chain termini. Transcription by E. coli RNA polymerase terminates efficiently at this site in vivo and in vitro, but transcription by T7 RNA polymerase is essentially unaffected. There are no primary cleavage sites for RNase III near the transcription termination site. The site of termination lies within HpaI fragment Q of T7 DNA, whose entire 446-nucleotide long sequence was determined. Cleavage sites for other restriction endonucleases are located conveniently for manipulating the DNA sequence around the termination site. The coding sequence for the last 82 amino acids of the T7 DNA ligase protein was identified, as was the beginning of a coding sequence for a possible late T7 protein from beyond the termination site.
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PMID:The transcription termination site at the end of the early region of bacteriophage T7 DNA. 700 54

Mammalian apurinic/apyrimidinic endonuclease 1 is a DNA repair enzyme involved in genome stability and expression of genes involved in oxidative stress responses, tumor progression and chemoresistance. However, the molecular mechanisms underlying the role of apurinic/apyrimidinic endonuclease 1 in these processes are still unclear. Recent findings point to a novel role of apurinic/apyrimidinic endonuclease 1 in RNA metabolism. Through the characterization of the interactomes of apurinic/apyrimidinic endonuclease 1 with RNA and other proteins, we demonstrate here a role for apurinic/apyrimidinic endonuclease 1 in pri-miRNA processing and stability via association with the DROSHA-processing complex during genotoxic stress. We also show that endonuclease activity of apurinic/apyrimidinic endonuclease 1 is required for the processing of miR-221/222 in regulating expression of the tumor suppressor PTEN. Analysis of a cohort of different cancers supports the relevance of our findings for tumor biology. We also show that apurinic/apyrimidinic endonuclease 1 participates in RNA-interactomes and protein-interactomes involved in cancer development, thus indicating an unsuspected post-transcriptional effect on cancer genes.APE1 plays an important role in the cellular response to oxidative stress, and mutations are linked to tumor progression and chemoresistance. Here, the authors characterize the interactions of APE1 with RNA and demonstrate a role in microRNA processing.
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PMID:Mammalian APE1 controls miRNA processing and its interactome is linked to cancer RNA metabolism. 2898 22