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Bacterial DNA binding protein information


Bac_DNA_binding
anabaena hu-dna cocrystal structure (ahu6)
Identifiers
SymbolBac_DNA_binding
PfamPF00216
InterProIPR000119
PROSITEPDOC00044
SCOP21hue / SCOPe / SUPFAM
CDDcd00591
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

In molecular biology, bacterial DNA binding proteins are a family of small, usually basic proteins of about 90 residues that bind DNA and are known as histone-like proteins.[1][2] Since bacterial binding proteins have a diversity of functions, it has been difficult to develop a common function for all of them. They are commonly referred to as histone-like and have many similar traits with the eukaryotic histone proteins. Eukaryotic histones package DNA to help it to fit in the nucleus, and they are known to be the most conserved proteins in nature.[3] Examples include the HU protein in Escherichia coli, a dimer of closely related alpha and beta chains and in other bacteria can be a dimer of identical chains. HU-type proteins have been found in a variety of bacteria (including cyanobacteria) and archaea, and are also encoded in the chloroplast genome of some algae.[4] The integration host factor (IHF), a dimer of closely related chains which is suggested to function in genetic recombination as well as in translational and transcriptional control[5] is found in Enterobacteria and viral proteins including the African swine fever virus protein A104R (or LMW5-AR).[6]

This family is also found in a group of eukaryotes known as dinoflagellates. These dinoflagellate histone-like proteins replace histone in some dinoflagellates and package DNA into a liquid-crystalline state.[7]

  1. ^ Drlica K, Rouviere-Yaniv J (September 1987). "Histonelike proteins of bacteria". Microbiological Reviews. 51 (3): 301–19. doi:10.1128/MMBR.51.3.301-319.1987. PMC 373113. PMID 3118156.
  2. ^ Pettijohn DE (September 1988). "Histone-like proteins and bacterial chromosome structure". The Journal of Biological Chemistry. 263 (26): 12793–6. doi:10.1016/S0021-9258(18)37625-7. PMID 3047111.
  3. ^ Griffiths, Anthony; Wessler, Susan; Carroll, Sean; Doebly, John. Introduction to Genetic Analysis (10 ed.). New York: W. H. Freeman and Company. pp. 428–429.
  4. ^ Wang SL, Liu XQ (December 1991). "The plastid genome of Cryptomonas phi encodes an hsp70-like protein, a histone-like protein, and an acyl carrier protein". Proceedings of the National Academy of Sciences of the United States of America. 88 (23): 10783–7. Bibcode:1991PNAS...8810783W. doi:10.1073/pnas.88.23.10783. PMC 53015. PMID 1961745.
  5. ^ Friedman DI (November 1988). "Integration host factor: a protein for all reasons" (PDF). Cell. 55 (4): 545–54. doi:10.1016/0092-8674(88)90213-9. hdl:2027.42/27063. PMID 2972385. S2CID 8548040.
  6. ^ Neilan JG, Lu Z, Kutish GF, Sussman MD, Roberts PC, Yozawa T, Rock DL (March 1993). "An African swine fever virus gene with similarity to bacterial DNA binding proteins, bacterial integration host factors, and the Bacillus phage SPO1 transcription factor, TF1". Nucleic Acids Research. 21 (6): 1496. doi:10.1093/nar/21.6.1496. PMC 309344. PMID 8464748.
  7. ^ Riaz, S; Sui, Z; Niaz, Z; Khan, S; Liu, Y; Liu, H (14 December 2018). "Distinctive Nuclear Features of Dinoflagellates with A Particular Focus on Histone and Histone-Replacement Proteins". Microorganisms. 6 (4): 128. doi:10.3390/microorganisms6040128. PMC 6313786. PMID 30558155.

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