Journal article
Assembly of the bacteriophage T4 primosome: Single-molecule and ensemble studies
Proceedings of the National Academy of Sciences - PNAS, v 102(9), pp 3254-3259
01 Mar 2005
PMID: 15728347
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Within replisomes for DNA replication, the primosome is responsible for unwinding double-stranded DNA and synthesizing RNA primers. Assembly of the bacteriophage T4 primosome on individual molecules of ssDNA or forked DNA (fDNA) has been studied by using FRET microscopy. On either DNA substrate, an ordered process of assembly begins with tight 1:1 binding of ssDNA-binding protein (gp32) and helicase-loading protein (gp59) to the DNA. Magnesium adenosine 5′-
O
-(3-thiotriphosphate) (MgATPγS) mediates the weak binding of helicase (gp41) to DNA coated with gp32 and gp59, whereas MgATP induces gp32 and gp59 to dissociate, leaving gp41 bound to the DNA. Finally, primase (gp61) binds to the gp41·DNA complex. Ensemble studies were used to determine protein stoichiometries and binding constants. These single-molecule studies provide an unambiguous description of the pathway for assembly of the primosome on the lagging strand of DNA at a replication fork.
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Details
- Title
- Assembly of the bacteriophage T4 primosome: Single-molecule and ensemble studies
- Creators
- Zhiquan Zhang - Department of Biochemistry, Duke University Medical Center, Box 3711, Durham, NC 27710; andMichelle M Spiering - Department of Biochemistry, Duke University Medical Center, Box 3711, Durham, NC 27710; andMichael A Trakselis - Department of Biochemistry, Duke University Medical Center, Box 3711, Durham, NC 27710; andFaoud T Ishmael - Department of Biochemistry, Duke University Medical Center, Box 3711, Durham, NC 27710; andJun Xi - Department of Biochemistry, Duke University Medical Center, Box 3711, Durham, NC 27710; andStephen J Benkovic - Department of Biochemistry, Duke University Medical Center, Box 3711, Durham, NC 27710; andGordon G Hammes - Department of Biochemistry, Duke University Medical Center, Box 3711, Durham, NC 27710; and
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, v 102(9), pp 3254-3259
- Publisher
- National Academy of Sciences
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Web of Science ID
- WOS:000227423700018
- Scopus ID
- 2-s2.0-14744278444
- Other Identifier
- 991014877690204721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology