Comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda - PubMed (original) (raw)
Comparative Study
Comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda
D H Ohlendorf et al. J Mol Biol. 1983.
Abstract
The three-dimensional structures of cro repressor protein and of the amino-terminal domain of lambda repressor protein, both from bacteriophage lambda, are compared. The second and third alpha-helices, alpha 2 and alpha 3, are shown to have essentially identical conformations in the two proteins, confirming the significance of the amino acid sequence homology previously noted between these and other DNA binding proteins in the region corresponding to these helices. The correspondence between the two-helical units in cro and lambda repressor protein is better than the striking agreement noted previously between two-helical units in cro and catabolite gene-activator protein. Parts of the first alpha-helices of repressor and cro show a structural correspondence that suggests a revised sequence homology between the two proteins in their extreme amino-terminal regions. In particular, there is a short loop between the alpha 1 and alpha 2 helices of lambda repressor that is missing from cro. This structural difference may account for the observed differences found with different cros and repressors in the pattern of phosphates whose ethylation prevents the binding of these proteins to their specific recognition sites. Although the two proteins have strikingly similar alpha 2-alpha 3 helical units that are presumed to bind to DNA in an essentially similar manner, stereochemical restrictions prevent the alpha 2-alpha 3 units of the respective proteins aligning on the DNA in exactly the same way.
Similar articles
- How Cro and lambda-repressor distinguish between operators: the structural basis underlying a genetic switch.
Albright RA, Matthews BW. Albright RA, et al. Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3431-6. doi: 10.1073/pnas.95.7.3431. Proc Natl Acad Sci U S A. 1998. PMID: 9520383 Free PMC article. - High resolution structural studies of Cro repressor protein and implications for DNA recognition.
Ohlendorf DH, Anderson WF, Takeda Y, Matthews BW. Ohlendorf DH, et al. J Biomol Struct Dyn. 1983 Oct;1(2):553-63. doi: 10.1080/07391102.1983.10507461. J Biomol Struct Dyn. 1983. PMID: 6400887 - Structural similarity in the DNA-binding domains of catabolite gene activator and cro repressor proteins.
Steitz TA, Ohlendorf DH, McKay DB, Anderson WF, Matthews BW. Steitz TA, et al. Proc Natl Acad Sci U S A. 1982 May;79(10):3097-100. doi: 10.1073/pnas.79.10.3097. Proc Natl Acad Sci U S A. 1982. PMID: 6212926 Free PMC article. - Protein-DNA recognition.
Pabo CO, Sauer RT. Pabo CO, et al. Annu Rev Biochem. 1984;53:293-321. doi: 10.1146/annurev.bi.53.070184.001453. Annu Rev Biochem. 1984. PMID: 6236744 Review. - lambda Repressor and cro--components of an efficient molecular switch.
Johnson AD, Poteete AR, Lauer G, Sauer RT, Ackers GK, Ptashne M. Johnson AD, et al. Nature. 1981 Nov 19;294(5838):217-23. doi: 10.1038/294217a0. Nature. 1981. PMID: 6457992 Review.
Cited by
- Tn10 tet operator mutations affecting Tet repressor recognition.
Wissmann A, Meier I, Wray LV Jr, Geissendörfer M, Hillen W. Wissmann A, et al. Nucleic Acids Res. 1986 May 27;14(10):4253-66. doi: 10.1093/nar/14.10.4253. Nucleic Acids Res. 1986. PMID: 3086838 Free PMC article. - A model for the non-specific binding of catabolite gene activator protein to DNA.
Weber IT, Steitz TA. Weber IT, et al. Nucleic Acids Res. 1984 Nov 26;12(22):8475-87. doi: 10.1093/nar/12.22.8475. Nucleic Acids Res. 1984. PMID: 6390343 Free PMC article. - Viral communities of the human gut: metagenomic analysis of composition and dynamics.
Aggarwala V, Liang G, Bushman FD. Aggarwala V, et al. Mob DNA. 2017 Oct 3;8:12. doi: 10.1186/s13100-017-0095-y. eCollection 2017. Mob DNA. 2017. PMID: 29026445 Free PMC article. Review. - How Cro and lambda-repressor distinguish between operators: the structural basis underlying a genetic switch.
Albright RA, Matthews BW. Albright RA, et al. Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3431-6. doi: 10.1073/pnas.95.7.3431. Proc Natl Acad Sci U S A. 1998. PMID: 9520383 Free PMC article. - Phage lambda Cro protein and cI repressor use two different patterns of specific protein-DNA interactions to achieve sequence specificity in vivo.
Benson N, Youderian P. Benson N, et al. Genetics. 1989 Jan;121(1):5-12. doi: 10.1093/genetics/121.1.5. Genetics. 1989. PMID: 2521838 Free PMC article.