Switch-like control of helicase processivity by single-stranded DNA binding protein

• Published in: eLife Vol. 10
• Main Authors: Stekas, Barbara, Yeo, Steve, Troitskaia, Alice, Honda, Masayoshi, Sho, Sei, Spies, Maria, Chemla, Yann R
• Format: Journal Article
• Language: English
• Published: England eLife Science Publications, Ltd 19.03.2021; eLife Sciences Publications Ltd; eLife Sciences Publications, Ltd
• Subjects: DNA; DNA binding proteins; DNA biosynthesis; DNA helicase; dna repair; Genomes; helicase; Hydrolysis; Molecular modelling; optical tweezers; Point mutation; Protein binding; Proteins; Replication protein A; single molecule; Single-stranded DNA; single-stranded DNA binding protein; Structural Biology and Molecular Biophysics; Unwinding; Xeroderma pigmentosum; XPD protein; single molecule; single-stranded DNA binding protein; optical tweezers; structural biology; dna repair; helicase; molecular biophysics

Helicases utilize nucleotide triphosphate (NTP) hydrolysis to translocate along single-stranded nucleic acids (NA) and unwind the duplex. In the cell, helicases function in the context of other NA-associated proteins such as single-stranded DNA binding proteins. Such encounters regulate helicase fun...