The single subunit RNA polymerases (ssRNAPs) of bacteriophages are highly interesting targets for the prediction and engineering of specific protein-DNA interactions. Despite extensive existing studies focusing on particular ssRNAPs such as the T7 RNAP, few rules governing the protein-DNA sequence covariations across diverse ssRNAPs and their cognate promoters are clearly known. Here, aiming to reveal such rules, we comprehensively mined promoters of various categories of ssRNAPs from phage genomes. For T7-like RNAPs, direct coupling analyses of the predicted set of RNAP-promoter pairs revealed that the interaction specificity was dominantly encoded by the amino acid and nucleotide residues at only a few key positions. The covariations between the amino acid and the nucleotide residues at these positions were summarized into a sparsely connected network. Using experimentally verified connections in this network, we designed a set of orthogonal T7 RNAP-promoter variants that showed more stringent orthogonality than previously reported sets. We further designed and experimentally verified variants with novel interactions. These results provided guidance for engineering novel RNAP-promoter pairs for synthetic biology or other applications. Our study also demonstrated the use of comprehensive genome mining in combination with sequence covariation analysis in the prediction and engineering of specific protein-DNA interactions.
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http://dx.doi.org/10.1093/nar/gkaf140 | DOI Listing |
Proc Natl Acad Sci U S A
March 2025
Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang 310030, China.
Mutations in the gene result in Nijmegen breakage syndrome (NBS), and the gene encodes NBS1 that forms a complex with MRE11 and RAD50 and participates in DNA damage repair. However, the molecular mechanism by which mutations cause clinical phenotypes of NBS, such as craniofacial dysmorphism, is still unclear. Here, we show that NBS1 localizes at the ribosomal DNA (rDNA) loci in nucleoli and interacts with ribosomal RNA (rRNA) transcription machinery including RNA polymerase I (Pol I) and TCOF1.
View Article and Find Full Text PDFJ Virol
March 2025
Joint Graduate School of Veterinary Sciences, Gifu University, Gifu, Japan.
Unlabelled: The rabies virus large (L) protein interacts with its cofactor phosphoprotein (P protein) to function as an RNA-dependent RNA polymerase (RdRp). The C-terminal domain (CTD) of the L protein plays a critical role in P protein binding. We previously reported that the highly conserved NPYNE sequence in the hydrophilic region of the CTD (positions 1929-1933 of the L protein [L1929-1933]) is important for both P protein binding and RdRp function.
View Article and Find Full Text PDFChemistry
March 2025
Wroclaw University of Science and Technology Faculty of Chemistry, Chemistry, Wybrzeże Stanisława Wyspiańskiego 27, 50-370 Wrocław, 50-370, Wrocław, POLAND.
During transcription, replication, and DNA repair, DNA unwinds to reveal guanine-rich sequences that form stable G-quadruplexes. In cancer cells, increased transcription and replication promote G4 formation, making them attractive therapeutic targets. G4s block DNA and RNA polymerases, inducing replication stress and causing toxic single- and double-strand breaks.
View Article and Find Full Text PDFDouble-strand breaks (DSBs) are toxic lesions that lead to genome instability. While canonical DSB repair pathways typically operate independently of RNA, emerging evidence suggests that RNA:DNA hybrids and transcripts near damaged sites can influence repair outcomes. However, a direct role for transcript RNA as a template during DSB repair in human cells is yet to be established.
View Article and Find Full Text PDFSci Data
March 2025
Department of Clinical Laboratory, Shenshan Central Hospital, Sun Yat-sen Memorial Hospital, Sun Yat-sen University, Shanwei, 516600, China.
A comprehensive dataset detailing protein interactors for the PARP family has been generated using TurboID proximity labeling under standardized experimental conditions. V5-TurboID fusion constructs enabled identification of 6,314 high-confidence interacting proteins through mass spectrometry, capturing transient interactions undetectable by conventional methods. Parallel GFP-PARP localization experiments validated physiological subcellular distributions.
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