dGTPase

Contributors: Aude Bernheim

Description

dGTPase is a family of proteins discovered in (N/A) . It degrades dGTP into phosphate-free deoxyguanosine. It was suggested that these "bacterial defensive proteins deplete deoxynucleotides_ from the_ nucleotide pool during phage infection, thus starving the phage of an essential DNA building block and halting its replication". The mechanism is remindful of the mechanism of SAMHD1 in humans.

Molecular mechanism

dGTPase degrades dGTP into phosphate-free deoxyguanosine. Phage mutants that overcome this defense carry mutations in phage-RNAP-modifying proteins suggesting, that "phage-mediated inhibition of host transcription may be involved in triggering the activation of bacterial dNTP-depletion".

Example of genomic structure

The dGTPase is composed of 1 protein: Sp_dGTPase.

Here is an example found in the RefSeq database:

dgtpase

The dGTPase system in Citrobacter sp. RHBSTW-00986 (GCF_013783065.1, NZ_CP056202) is composed of 1 protein: Sp_dGTPase (WP_048216953.1)

Distribution of the system among prokaryotes

Structure

Experimental validation