From Wikipedia, the free encyclopedia
CsrA
CsrA dimer from Escherichia coli. [1]
Identifiers
SymbolCsrA
Pfam PF02599
InterPro IPR003751
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Carbon storage regulator A (CsrA) is an RNA binding protein. The CsrA homologs are found in most bacterial species, in the pseudomonads they are called repressor of secondary metabolites (RsmA and RsmE). [2] The CsrA proteins generally bind to the Shine-Dalgarno sequence of messenger RNAs and either inhibit translation or facilitate mRNA decay. [3]

CsrA has a regulatory effect on glycogen biosynthesis and catabolism, glycolysis, [3] biofilm formation [4] and quorum sensing. [5]

Interactions

A consensus secondary structure and primary sequence for the targets of the CsrA RNA binding protein.

The CsrA protein binds to a Stem-loop RNA motif. The ability of the protein to inhibit translation of bound mRNAs can be countered by the expression of sRNAs such as CsrB, CsrC, RsmZ, RsmY and RsmX that contain multiple copies of the RNA motif. These RNAs sequester CsrA, which allows the translation of the previously inhibited bound mRNAs. A study investigating specific binding of CsrA in the Salmonella transcriptome has identified 467 binding sites. [6]

References

  1. ^ Gutiérrez, P; Li, Y; Osborne, MJ; Pomerantseva, E; Liu, Q; Gehring, K (May 2005). "Solution structure of the carbon storage regulator protein CsrA from Escherichia coli". Journal of Bacteriology. 187 (10): 3496–501. doi: 10.1128/JB.187.10.3496-3501.2005. PMC  1112004. PMID  15866937.
  2. ^ Timmermans, J; Van Melderen, L (Sep 2010). "Post-transcriptional global regulation by CsrA in bacteria". Cellular and Molecular Life Sciences. 67 (17): 2897–908. doi: 10.1007/s00018-010-0381-z. PMC  11115721. PMID  20446015. S2CID  23366724.
  3. ^ a b Liu, MY; Gui, G; Wei, B; Preston JF, 3rd; Oakford, L; Yüksel, U; Giedroc, DP; Romeo, T (Jul 11, 1997). "The RNA molecule CsrB binds to the global regulatory protein CsrA and antagonizes its activity in Escherichia coli". The Journal of Biological Chemistry. 272 (28): 17502–10. doi: 10.1074/jbc.272.28.17502. PMID  9211896.{{ cite journal}}: CS1 maint: numeric names: authors list ( link)
  4. ^ Jackson, DW; Suzuki, K; Oakford, L; Simecka, JW; Hart, ME; Romeo, T (Jan 2002). "Biofilm formation and dispersal under the influence of the global regulator CsrA of Escherichia coli". Journal of Bacteriology. 184 (1): 290–301. doi: 10.1128/jb.184.1.290-301.2002. PMC  134780. PMID  11741870.
  5. ^ Sonnleitner, E; Romeo, A; Bläsi, U (Apr 2012). "Small regulatory RNAs in Pseudomonas aeruginosa". RNA Biology. 9 (4): 364–71. doi: 10.4161/rna.19231. PMID  22336763.
  6. ^ Holmqvist E, Wright PR, Li L, Bischler T, Barquist L, Reinhardt R, Backofen R, Vogel J (2016). "Global RNA recognition patterns of post-transcriptional regulators Hfq and CsrA revealed by UV crosslinking in vivo". EMBO J. 35 (9): 991–1011. doi: 10.15252/embj.201593360. PMC  5207318. PMID  27044921.
From Wikipedia, the free encyclopedia
CsrA
CsrA dimer from Escherichia coli. [1]
Identifiers
SymbolCsrA
Pfam PF02599
InterPro IPR003751
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Carbon storage regulator A (CsrA) is an RNA binding protein. The CsrA homologs are found in most bacterial species, in the pseudomonads they are called repressor of secondary metabolites (RsmA and RsmE). [2] The CsrA proteins generally bind to the Shine-Dalgarno sequence of messenger RNAs and either inhibit translation or facilitate mRNA decay. [3]

CsrA has a regulatory effect on glycogen biosynthesis and catabolism, glycolysis, [3] biofilm formation [4] and quorum sensing. [5]

Interactions

A consensus secondary structure and primary sequence for the targets of the CsrA RNA binding protein.

The CsrA protein binds to a Stem-loop RNA motif. The ability of the protein to inhibit translation of bound mRNAs can be countered by the expression of sRNAs such as CsrB, CsrC, RsmZ, RsmY and RsmX that contain multiple copies of the RNA motif. These RNAs sequester CsrA, which allows the translation of the previously inhibited bound mRNAs. A study investigating specific binding of CsrA in the Salmonella transcriptome has identified 467 binding sites. [6]

References

  1. ^ Gutiérrez, P; Li, Y; Osborne, MJ; Pomerantseva, E; Liu, Q; Gehring, K (May 2005). "Solution structure of the carbon storage regulator protein CsrA from Escherichia coli". Journal of Bacteriology. 187 (10): 3496–501. doi: 10.1128/JB.187.10.3496-3501.2005. PMC  1112004. PMID  15866937.
  2. ^ Timmermans, J; Van Melderen, L (Sep 2010). "Post-transcriptional global regulation by CsrA in bacteria". Cellular and Molecular Life Sciences. 67 (17): 2897–908. doi: 10.1007/s00018-010-0381-z. PMC  11115721. PMID  20446015. S2CID  23366724.
  3. ^ a b Liu, MY; Gui, G; Wei, B; Preston JF, 3rd; Oakford, L; Yüksel, U; Giedroc, DP; Romeo, T (Jul 11, 1997). "The RNA molecule CsrB binds to the global regulatory protein CsrA and antagonizes its activity in Escherichia coli". The Journal of Biological Chemistry. 272 (28): 17502–10. doi: 10.1074/jbc.272.28.17502. PMID  9211896.{{ cite journal}}: CS1 maint: numeric names: authors list ( link)
  4. ^ Jackson, DW; Suzuki, K; Oakford, L; Simecka, JW; Hart, ME; Romeo, T (Jan 2002). "Biofilm formation and dispersal under the influence of the global regulator CsrA of Escherichia coli". Journal of Bacteriology. 184 (1): 290–301. doi: 10.1128/jb.184.1.290-301.2002. PMC  134780. PMID  11741870.
  5. ^ Sonnleitner, E; Romeo, A; Bläsi, U (Apr 2012). "Small regulatory RNAs in Pseudomonas aeruginosa". RNA Biology. 9 (4): 364–71. doi: 10.4161/rna.19231. PMID  22336763.
  6. ^ Holmqvist E, Wright PR, Li L, Bischler T, Barquist L, Reinhardt R, Backofen R, Vogel J (2016). "Global RNA recognition patterns of post-transcriptional regulators Hfq and CsrA revealed by UV crosslinking in vivo". EMBO J. 35 (9): 991–1011. doi: 10.15252/embj.201593360. PMC  5207318. PMID  27044921.

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