D
IPR015085

Bacteriophage T4, Gp59, helicase assembly protein, N-terminal

InterPro entry
Short namePhage_T4_Gp59_N
Overlapping
homologous
superfamilies
 

Description

The Bacteriophage T4 gene 59 helicase assembly protein (Gp59) is required for recombination-dependent DNA replication and repair, which is the predominant mode of DNA replication in the late stage of T4 infection. Gp59 accelerates the loading of the T4 gene 41 helicase during DNA synthesis by the T4 replication system in vitro. This protein binds to both T4 gene 41 helicase and T4 gene 32 single-stranded DNA binding protein, and to single and double-stranded DNA
[2]
.

The structure of Gp59 helicase assembly protein reveals a novel α-helical bundle fold with two domains of similar size. Surface residues are predominantly basic (pI 9.37) with clusters of acidic residues but exposed hydrophobic residues suggest sites for potential contact with DNA and with other protein molecules
[1]
. The N-terminal domain shares structural homology with the high mobility group (HMG) proteins from eukaryotic organisms and it has been suggested that it plays a role in duplex DNA binding ahead of the fork. The C-terminal domain interacts with the helicase (T4 gp41) and with SSB (single-stranded binding protein T4 gp32)
[2]
.

References

1.Bacteriophage T4 gene 59 helicase assembly protein binds replication fork DNA. The 1.45 A resolution crystal structure reveals a novel alpha-helical two-domain fold. Mueser TC, Jones CE, Nossal NG, Hyde CC. J. Mol. Biol. 296, 597-612, (2000). View articlePMID: 10669611

2.Mutational analysis of the T4 gp59 helicase loader reveals its sites for interaction with helicase, single-stranded binding protein, and DNA. Dolezal D, Jones CE, Lai X, Brister JR, Mueser TC, Nossal NG, Hinton DM. J Biol Chem 287, 18596-607, (2012). PMID: 22427673

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