Unknown

Dataset Information

0

Inferring primase-DNA specific recognition using a data driven approach.


ABSTRACT: DNA-protein interactions play essential roles in all living cells. Understanding of how features embedded in the DNA sequence affect specific interactions with proteins is both challenging and important, since it may contribute to finding the means to regulate metabolic pathways involving DNA-protein interactions. Using a massive experimental benchmark dataset of binding scores for DNA sequences and a machine learning workflow, we describe the binding to DNA of T7 primase, as a model system for specific DNA-protein interactions. Effective binding of T7 primase to its specific DNA recognition sequences triggers the formation of RNA primers that serve as Okazaki fragment start sites during DNA replication.

SUBMITTER: Soffer A 

PROVIDER: S-EPMC8599759 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Inferring primase-DNA specific recognition using a data driven approach.

Soffer Adam A   Eisdorfer Sarah A SA   Ifrach Morya M   Ilic Stefan S   Afek Ariel A   Schussheim Hallel H   Vilenchik Dan D   Akabayov Barak B  

Nucleic acids research 20211101 20


DNA-protein interactions play essential roles in all living cells. Understanding of how features embedded in the DNA sequence affect specific interactions with proteins is both challenging and important, since it may contribute to finding the means to regulate metabolic pathways involving DNA-protein interactions. Using a massive experimental benchmark dataset of binding scores for DNA sequences and a machine learning workflow, we describe the binding to DNA of T7 primase, as a model system for  ...[more]

Similar Datasets

| S-EPMC4366811 | biostudies-other
| S-EPMC16326 | biostudies-literature
| S-EPMC5737085 | biostudies-literature
| S-EPMC5071827 | biostudies-literature
| S-EPMC9029400 | biostudies-literature
| S-EPMC1865582 | biostudies-literature
| S-EPMC11191566 | biostudies-literature
| S-EPMC5223348 | biostudies-literature
| S-EPMC2141844 | biostudies-literature
| S-EPMC10727444 | biostudies-literature