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Structure of lambda CII: implications for recognition of direct-repeat DNA by an unusual tetrameric organization.

Datta AB, Panjikar S, Weiss MS, Chakrabarti P, Parrack P
Proc Natl Acad Sci U S A 102 11242-7 (2005)
Cited: 13 times
EuropePMC logo PMID: 16061804

Abstract

The temperate coliphage lambda, after infecting its host bacterium Escherichia coli, can develop either along the lytic or the lysogenic pathway. Crucial to the lysis/lysogeny decision is the homotetrameric transcription-activator protein CII (4 x 11 kDa) of the phage that binds to a unique direct-repeat sequence T-T-G-C-N6-T-T-G-C at each of the three phage promoters it activates: p(E), p(I), and p(aQ). Several regions of CII have been identified for its various functions (DNA binding, oligomerization, and susceptibility to host protease), but the crystal structure of the protein long remained elusive. Here, we present the three-dimensional structure of CII at 2.6-angstroms resolution. The CII monomer is comprised of four alpha helices and a disordered C terminus. The first three helices (alpha1-alpha3) form a compact domain, whereas the fourth helix (alpha4) protrudes in different orientations in each subunit. A four-helix bundle, formed by alpha4 from each subunit, holds the tetramer. The quaternary structure can be described as a dimer of dimers, but the tetramer does not exhibit a closed symmetry. This unusual quaternary arrangement allows the placement of the helix-turn-helix motifs of two of the four CII subunits for interaction with successive major grooves of B-DNA, from one face of DNA. This structure provides a simple explanation for how a homotetrameric protein may recognize a direct-repeat DNA sequence rather than the inverted-repeat sequences of most prokaryotic activators.

Articles - 1xwr mentioned but not cited (3)

  1. The protein interaction map of bacteriophage lambda. Rajagopala SV, Casjens S, Uetz P. BMC Microbiol 11 213 (2011)
  2. Structure of lambda CII: implications for recognition of direct-repeat DNA by an unusual tetrameric organization. Datta AB, Panjikar S, Weiss MS, Chakrabarti P, Parrack P. Proc Natl Acad Sci U S A 102 11242-11247 (2005)
  3. Crystallization and X-ray analysis of the transcription-activator protein C1 of bacteriophage P22 in complex with the PRE promoter element. Mondal A, Chattopadhyaya R, Datta AB, Parrack P. Acta Crystallogr F Struct Biol Commun 71 1286-1291 (2015)


Reviews citing this publication (1)

  1. Hybrid Vigor: Importance of Hybrid λ Phages in Early Insights in Molecular Biology. Feiss M, Young R, Ramsey J, Adhya S, Georgopoulos C, Hendrix RW, Hatfull GF, Gilcrease EB, Casjens SR. Microbiol Mol Biol Rev 86 e0012421 (2022)

Articles citing this publication (9)

  1. Lysis-lysogeny coexistence: prophage integration during lytic development. Shao Q, Trinh JT, McIntosh CS, Christenson B, Balázsi G, Zeng L. Microbiologyopen 6 (2017)
  2. Identification of a divided genome for VSH-1, the prophage-like gene transfer agent of Brachyspira hyodysenteriae. Stanton TB, Humphrey SB, Bayles DO, Zuerner RL. J Bacteriol 191 1719-1721 (2009)
  3. Induction and transcription of VSH-1, a prophage-like gene transfer agent of Brachyspira hyodysenteriae. Matson EG, Zuerner RL, Stanton TB. Anaerobe 13 89-97 (2007)
  4. Crystal structure of the P2 C-repressor: a binder of non-palindromic direct DNA repeats. Massad T, Skaar K, Nilsson H, Damberg P, Henriksson-Peltola P, Haggård-Ljungquist E, Högbom M, Stenmark P. Nucleic Acids Res 38 7778-7790 (2010)
  5. HflD, an Escherichia coli protein involved in the lambda lysis-lysogeny switch, impairs transcription activation by lambdaCII. Parua PK, Mondal A, Parrack P. Arch Biochem Biophys 493 175-183 (2010)
  6. Specific hydrophobic residues in the alpha4 helix of lambdaCII are crucial for maintaining its tetrameric structure and directing the lysogenic choice. Parua PK, Datta AB, Parrack P. J Gen Virol 91 306-312 (2010)
  7. Induction and Genomic Analysis of a Lysogenic Phage of Hafnia paralvei. Pan L, Li D, Tong Y, Lin W, Qin W, Xu L, Zhan P. Curr Microbiol 79 50 (2022)
  8. Studies on Escherichia coli HflKC suggest the presence of an unidentified λ factor that influences the lysis-lysogeny switch. Bandyopadhyay K, Parua PK, Datta AB, Parrack P. BMC Microbiol 11 34 (2011)
  9. Structural basis of DNA binding by YdaT, a functional equivalent of the CII repressor in the cryptic prophage CP-933P from Escherichia coli O157:H7. Prolič-Kalinšek M, Volkov AN, Hadži S, Van Dyck J, Bervoets I, Charlier D, Loris R. Acta Crystallogr D Struct Biol 79 245-258 (2023)


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