Nucleoid-associated protein Lsr2


Nucleoid-associated protein Lsr2
Not Available
Gene Name
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0052071|Nucleoid-associated protein Lsr2
Number of residues
Molecular Weight
Theoretical pI
Not Available
GO Classification
DNA binding
cellular response to oxygen levels / DNA protection / pathogenesis / regulation of transcription, DNA-templated / response to hydrogen peroxide / response to iron ion
cell wall / cytosol / nucleoid / plasma membrane
General Function
DNA-bridging protein that has both architectural and regulatory roles (PubMed:18187505). Influences the organization of chromatin and gene expression by binding non-specifically to DNA, with a preference for AT-rich sequences, and bridging distant DNA segments (PubMed:20133735). Binds in the minor groove of AT-rich DNA (PubMed:21673140). Represses expression of multiple genes involved in a broad range of cellular processes, including major virulence factors or antibiotic-induced genes, such as iniBAC or efpA (PubMed:17590082), and genes important for adaptation of changing O(2) levels (PubMed:24895305). May also activate expression of some gene (PubMed:24895305). May coordinate global gene regulation and virulence (PubMed:20133735). Also protects mycobacteria against reactive oxygen intermediates during macrophage infection by acting as a physical barrier to DNA degradation (PubMed:19237572); the physical protection has been questioned (PubMed:24895305). A strain overexpressing this protein consumes O(2) more slowly than wild-type (PubMed:24895305).
Specific Function
Dna binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Gene sequence
>lcl|BSEQ0052072|Nucleoid-associated protein Lsr2 (lsr2)
Chromosome Location
Not Available
Not Available
External Identifiers
UniProtKB Entry NameLSR2_MYCTU
General References
  1. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
  2. Colangeli R, Helb D, Vilcheze C, Hazbon MH, Lee CG, Safi H, Sayers B, Sardone I, Jones MB, Fleischmann RD, Peterson SN, Jacobs WR Jr, Alland D: Transcriptional regulation of multi-drug tolerance and antibiotic-induced responses by the histone-like protein Lsr2 in M. tuberculosis. PLoS Pathog. 2007 Jun;3(6):e87. doi: 10.1371/journal.ppat.0030087. [Article]
  3. Chen JM, Ren H, Shaw JE, Wang YJ, Li M, Leung AS, Tran V, Berbenetz NM, Kocincova D, Yip CM, Reyrat JM, Liu J: Lsr2 of Mycobacterium tuberculosis is a DNA-bridging protein. Nucleic Acids Res. 2008 Apr;36(7):2123-35. doi: 10.1093/nar/gkm1162. Epub 2008 Jan 10. [Article]
  4. Colangeli R, Haq A, Arcus VL, Summers E, Magliozzo RS, McBride A, Mitra AK, Radjainia M, Khajo A, Jacobs WR Jr, Salgame P, Alland D: The multifunctional histone-like protein Lsr2 protects mycobacteria against reactive oxygen intermediates. Proc Natl Acad Sci U S A. 2009 Mar 17;106(11):4414-8. doi: 10.1073/pnas.0810126106. Epub 2009 Feb 23. [Article]
  5. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
  6. Gordon BR, Li Y, Cote A, Weirauch MT, Ding P, Hughes TR, Navarre WW, Xia B, Liu J: Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins. Proc Natl Acad Sci U S A. 2011 Jun 28;108(26):10690-5. doi: 10.1073/pnas.1102544108. Epub 2011 Jun 14. [Article]
  7. Bartek IL, Woolhiser LK, Baughn AD, Basaraba RJ, Jacobs WR Jr, Lenaerts AJ, Voskuil MI: Mycobacterium tuberculosis Lsr2 is a global transcriptional regulator required for adaptation to changing oxygen levels and virulence. MBio. 2014 Jun 3;5(3):e01106-14. doi: 10.1128/mBio.01106-14. [Article]
  8. Gordon BR, Li Y, Wang L, Sintsova A, van Bakel H, Tian S, Navarre WW, Xia B, Liu J: Lsr2 is a nucleoid-associated protein that targets AT-rich sequences and virulence genes in Mycobacterium tuberculosis. Proc Natl Acad Sci U S A. 2010 Mar 16;107(11):5154-9. doi: 10.1073/pnas.0913551107. Epub 2010 Jan 20. [Article]
  9. Summers EL, Meindl K, Uson I, Mitra AK, Radjainia M, Colangeli R, Alland D, Arcus VL: The structure of the oligomerization domain of Lsr2 from Mycobacterium tuberculosis reveals a mechanism for chromosome organization and protection. PLoS One. 2012;7(6):e38542. doi: 10.1371/journal.pone.0038542. Epub 2012 Jun 13. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails