| Description | This entry represents Lsr2, which is a small, basic DNA-binding protein present in Mycobacterium and related actinomycetes that regulates gene expression and influences the organization of bacterial chromatin. Lsr2 is a dimer that binds to AT-rich regions of chromosomal DNA and physically protects DNA from damage by reactive oxygen intermediates (ROI). It is a functional homologue of the H-NS-like proteins [ ]. H-NS proteins play a role in nucleoid organisation and also function as a pleiotropic regulator of gene expression [, ].The Lsr2 protein is composed of two domains. The N-terminal domain mediates the dimerization of Lsr2 [ ]. The C-terminal DNA-binding domain of Lsr2 interacts with the minor groove of DNA, and shares similarity to other bacterial nucleoid-associated DNA-binding domains []. The C-terminal domain is found associated with a variety of other protein domains (such as Ku and Ribonuclease T) where it presumably provides a DNA-binding activity. | Name | Lsr2 |
| Short Name | Lsr2 | Type | Family |
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