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Rv0802c acetyltransferase from Mycobacterium tuberculosis H37Rv.

L Kovács¹, Agnes Csanádi, Eva Kiss

¹Department of Medical Microbiology and Immunobiology, University of Szeged, Hungary.

Acta Microbiologica Et Immunologica Hungarica

|January 13, 2006

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Rv0802c acetyltransferase, a protein associated with mycobacterial RNase E, was identified in Mycobacterium tuberculosis. This 25 kDa enzyme exhibits sequence homology with other acetyltransferases and contains a key motif for acetyl-coenzyme A binding.

Area of Science:

Microbiology
Biochemistry
Molecular Biology

Background:

Rv0802c is identified as an acetyltransferase linked to RNase E in mycobacteria.
Mycobacterium tuberculosis is a significant pathogen requiring detailed molecular study.

Purpose of the Study:

To characterize the Rv0802c acetyltransferase from Mycobacterium tuberculosis.
To investigate the biochemical properties and potential function of Rv0802c.

Main Methods:

Cloning of the 6His and FLAG-tagged Rv0802c gene from Mycobacterium tuberculosis H37Rv.
Expression of the recombinant protein in Escherichia coli.
Partial purification of the 25 kDa acetyltransferase.

Main Results:

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The Rv0802c protein was successfully expressed and partially purified.

A molecular weight of 25 kDa was determined for the enzyme.

Sequence analysis revealed modest homology with known acetyltransferases.

The characteristic R-X-X-G-X-G motif, crucial for acetyl-coenzyme A binding, was identified.

Conclusions:

Rv0802c is a functional acetyltransferase in Mycobacterium tuberculosis.
The identified protein likely plays a role in acetylation processes within the bacterium.
Further studies are warranted to elucidate its specific function and interaction with RNase E.