Inside the MADS box

Article Abstract:

The N-terminal of the MCM1-Agamous-Deficiens-SRF (MADS) box present at the amino terminus of the DNA-binding proteins, the mammalian transcription factor SRF and its yeast relative MCM1, binds DNA while the residues present at the top of the protein bind accessory protein molecules. DNA binding may affect the accessory protein binding domains as they are in contact with the backbone of the DNA phosphate. MCM1 also contains some mutations in the MADS due to which it binds some sites normally but does not bind the accessory protein MAT-alpha-1.

Binding sites (Biochemistry), Active sites (Biochemistry)

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Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA

Article Abstract:

The crystal structure of the gp32 DNA binding domain complexed to single-stranded (ss)DNA reveals the presence of three structural subdomains and a positively charged surface that is parallel to hydrophobic pockets formed by aromatic side chains. The replication, recombination and repair of bacteriophage T4DNA requires ssDNA binding protein gp32. Gp32 binding affects many aspects of DNA metabolism, such as configuring ssDNA templates for efficient use, protecting exposed ssDNA from nucleases and removing unnecessary secondary structures.

Genetic aspects, Bacteriophages

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Interaction of E1 and hSNF5 proteins stimulates replication of human papillomavirus DNA

Article Abstract:

There is a direct link between E1-Ini1/hSNF5 binding and human papillomavirus DNA replication. E1 and SV40 large T antigen share amino-acid similarity in eight clear regions that form a significant binding domain for ATPase, DNA helicase and DNA polymerase-alpha. Proteins that regulate transcription by changing chromatin structure could be influential regulators of DNA replication too. The interaction of E1 with Ini1/hSNF5 could be a key phase in the initiation of viral DNA replication.

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