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Structural modeling of Gene 32 protein and SSB's roles in DNA replication, recombination and repair
Author(s) -
Rogers Katie,
Hobgood Mike,
Nance Jimia,
Cline Deborah,
Browning Stephanie,
Eason Mo'rease,
Eversburg Amber,
Lawson Nikki,
Campbell Linda,
Wilhelm Dayna,
Karpel Richard
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.lb48
Subject(s) - dna , replication protein a , hmg box , seqa protein domain , gene , dna replication , protein–dna interaction , dna binding protein , biology , genetics , chemistry , microbiology and biotechnology , origin of replication , transcription factor
Students participating in the Students Modeling a Research Topic (SMART) team partnership program involving Lackey High School, University of Maryland Baltimore County and Milwaukee School of Engineering used 3‐D printing technology to create a physical model of T4 bacteriophage gene 32 protein and researched its role in denaturation and renaturation of DNA. Gene 32 protein is a single‐stranded binding protein (SSB) that has three domains: the core domain with an OB fold provides a structural trough for binding single stranded DNA (ssDNA); the B domain (amino acids 1–21) is responsible for cooperatively interacting with the core domains of other SSBs; and the A domain (C‐terminal 48 amino acids) binds to other proteins of the replication machinery and acts as a gate keeper by mimicking DNA thus controlling DNA binding. Gene 32 protein binds weakly to double stranded DNA (dsDNA). It is theorized that a region on the protein surface rich in lysine residues electrostatically interacts with the phosphates in the dsDNA major groove. dsDNA interaction might provide a means by which the protein could rapidly one‐dimensionally diffuse to transient single stranded regions on the DNA, thus facilitating its roles in DNA replication, recombination and repair. Supported by a grant from HHMI.