Differential mobility of the N-terminal headpiece in the lac-repressor protein

Wade-Jardetzky, Norma G.; Bray, Ryan; Conover, Woodrow W.; Jardetzky, Oleg; Geisler, Norbert; Weber, Klaus

doi:10.1016/0022-2836(79)90129-3

Cited by 92 publications

(61 citation statements)

References 12 publications

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“…However, n.m.r. studies of intact repressor show that the 'headpiece' is rather mobile with respect to the ligand-binding domain (Wade-Jardetzky et al, 1979).…”

Section: Helix-turn-helix Proteinsmentioning

confidence: 99%

Structural aspects of protein-DNA recognition

Freemont

Lane

Sanderson

1991

Biochemical Journal

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“…However, n.m.r. studies of intact repressor show that the 'headpiece' is rather mobile with respect to the ligand-binding domain (Wade-Jardetzky et al, 1979).…”

Section: Helix-turn-helix Proteinsmentioning

confidence: 99%

Structural aspects of protein-DNA recognition

Freemont

Lane

Sanderson

1991

Biochemical Journal

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“…The headpiece fraction was rechromatographed on Sephadex G-50 superfine (2 X 90 cm bed for 5 mg 246 headpieces) and concentrated by ultrafiltration (Diaflo membranes UM02, Amicon Corp., Lexington). The mixture of short and long headpieces was employed for the studies since there is no indication of structural differences between the two different headpieces [ 5,6]. Headpiece concentration was determined using an absorption coefficient of A :trn 280 nm = 8.80.…”

Section: Methodsmentioning

confidence: 99%

lac‐Repressor headpiece constitutes a reversibly unfolding domain

1981

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“…Previously it had been shown [12,13] that the aromatic resonances of the headpiece in the NMR spectrum of whole repressor are much sharper than those of the core and have the same chemical shift positions as those of the free headpiece. This was interpreted as showing that headpiece constitutes a separate domain connected to the core with a flexible hinge region, which gives it a higher mobility than the rest of the molecule.…”

Section: Lac Repressormentioning

confidence: 99%

Photo‐CIDNP study of the interaction between lac repressor headpiece and lac operator DNA

et al. 1988

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L.uc repressor headpiece (HP) and intact lac repressor have been studied using the photo-CIDNP method. At neutral pH histidine 29, tyrosines 7, 12 and 17 and methionine 1 are polarised. His-29 polarisations are weaker and broader in HP59 than in HP51 indicating that the C-terminal octapeptide in HP59 adopts a conformation that allows an interaction with His-29. The photo-CIDNP spectra of intact lac repressor and HP51 are very similar, showing that the same residues are accessible to the photo-excited flavin. An equimolar mixture of HPSI and a 14 base pair lac operator fragment strongly suppresses the photo-CIDNP effect of tyrosines 7 and 17 and abolishes the His-29 polarisations. The results are compared with earlier photo-CIDNP measurements on a complex of headpiece with poly[d(AT)] and with a model derived from a 2D NMR study on a lac headpiece-operator complex.L,uc repressor; L.uc headpiece; Luc operator; L.uc headpiece-operator complex; Photo-CIDNP; 'H-NMR

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Differential mobility of the N-terminal headpiece in the lac-repressor protein

Cited by 92 publications

References 12 publications

Structural aspects of protein-DNA recognition

Structural aspects of protein-DNA recognition

lac‐Repressor headpiece constitutes a reversibly unfolding domain

Photo‐CIDNP study of the interaction between lac repressor headpiece and lac operator DNA

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