Molecular Dissection of the Homotrimeric Sliding Clamp of T4 Phage: Two Domains of a Subunit Display Asymmetric Characteristics
Author:
Affiliation:
1. Microbiology and Molecular Biology Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research (IISER), Bhopal 462023, India
Funder
Council of Scientific and Industrial Research
Science and Engineering Research Board
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b01204
Reference28 articles.
1. Two types of replication proteins increase the rate at which T4 DNA polymerase traverses the helical regions in a single-stranded DNA template.
2. DNA POLYMERASE III HOLOENZYME: Structure and Function of a Chromosomal Replicating Machine
3. Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp
4. The sliding clamp of DNA polymerase III holoenzyme encircles DNA.
5. Structural and functional similarities of prokaryotic and eukaryotic DNA polymerase sliding clamps
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1. From Processivity to Genome Maintenance: The Many Roles of Sliding Clamps;Genes;2022-11-07
2. Identification and Characterization of an Inside-Out Folding Intermediate of T4 Phage Sliding Clamp;Biophysical Journal;2017-10
3. Dissecting the structure-function relationship in lysozyme domain of mycobacteriophage D29-encoded peptidoglycan hydrolase;FEBS Letters;2017-09-20
4. On the domains of T4 phage sliding clamp gp45: An intermolecular crosstalk governs structural stability and biological activity;Biochimica et Biophysica Acta (BBA) - General Subjects;2017-01
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