Refined Structure of Repressor Headpiece (1-56) Determined by Relaxation Matrix Calculations from 2D and 3D NOE Data: Change of Tertiary Structure upon Binding to the Operator

Slijper, Monique; Bonvin, Alexandre M. J. J.; Boelens, Rolf; Kaptein, Robert

doi:10.1006/jmbi.1996.0356

Cited by 63 publications

(60 citation statements)

References 55 publications

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“…Thus, while the headpiece in the absence of nucleic acid (but in high salt concentration) revealed local regions of structure, these local structures were connected by very flexible loops , whereas the hinge region appeared to be completely disordered (Kercher et al, 1997). As a result of binding to DNA, the headpiece gains a rigid helix-turn-helix structure (Lewis et al, 1996;Slijper et al, 1996Slijper et al, , 1997, whereas the hinge region becomes ordered and forms an -helix (residues 50-58), which makes specific interaction with the operator DNA (Spronk et al, 1996;Kercher et al, 1997). When the hinge helix is formed in the repressor-DNA complex, it interacts with the hinge helix of its dimer partner, and, as a unit, the pair of hinge helices of a dimer binds in the minor groove of the DNA (Spronk et al, 1996; Kercher et al, 1997).…”

Section: Dna-binding Proteinsmentioning

confidence: 92%

Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling

2005

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Regulation, recognition and cell signaling involve the coordinated actions of many players. To achieve this coordination, each participant must have a valid identification (ID) that is easily recognized by the others. For proteins, these IDs are often within intrinsically disordered (also ID) regions. The functions of a set of well-characterized ID regions from a diversity of proteins are presented herein to support this view. These examples include both more recently described signaling proteins, such as p53, alpha-synuclein, HMGA, the Rieske protein, estrogen receptor alpha, chaperones, GCN4, Arf, Hdm2, FlgM, measles virus nucleoprotein, RNase E, glycogen synthase kinase 3beta, p21(Waf1/Cip1/Sdi1), caldesmon, calmodulin, BRCA1 and several other intriguing proteins, as well as historical prototypes for signaling, regulation, control and molecular recognition, such as the lac repressor, the voltage gated potassium channel, RNA polymerase and the S15 peptide associating with the RNA polymerase S-protein. The frequent occurrence and the common use of ID regions in important protein functions raise the possibility that the relationship between amino acid sequence, disordered ensemble and function might be the dominant paradigm for the molecular recognition that serves as the basis for signaling and regulation by protein molecules.

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Section: Dna-binding Proteinsmentioning

confidence: 92%

Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling

2005

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“…1) (7)(8)(9)(10). The N-terminal 60 amino acids in each monomer form a helix-turn-helix motif that directly contacts the operator DNA (7,(11)(12)(13)(14)(15)(16)(17). When isolated, this region exhibits site-specific DNA binding, albeit with significantly lower affinity than the intact protein (11,18,19).…”

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confidence: 99%

Glycine Insertion in the Hinge Region of Lactose Repressor Protein Alters DNA Binding

Falcon

Matthews

1999

Journal of Biological Chemistry

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Amino acid alterations were designed at the C terminus of the hinge segment (amino acids ϳ51-59 The lac repressor (LacI) negatively regulates lac mRNA synthesis by binding with high affinity to its target operator site and thereby precluding transcription by RNA polymerase (1-6). In response to the presence of inducer sugars, LacI undergoes a conformational change that results in diminished affinity for operator sequences without effect on nonspecific DNA binding (1, 2, 7). LacI is a protein of 150,000 Da composed of four identical subunits assembled as a dimer of dimers (see Fig.

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“…Function-In earlier studies (26), we identified the N-terminal region of hTS as a degron by ligating amino acids 1-45, spanning the IDR (residues 1-28) and an hA (residues [31][32][33][34][35][36][37][38][39][40][41][42], to the N terminus of eGFP. CHX chase analysis indicated that this protein, termed N30-hA-eGFP, has a half-life of ϳ9-10 h in transfected mammalian cells, as compared with Ͼ24 h for the parental eGFP reporter polypeptide (26).…”

Section: The Ha Helix At Residues 31-42 Of Hts Is Required For Degronmentioning

confidence: 99%

“…The Helix-Loop-Helix Motif of the lac Repressor Contributes to Degron Function-Structural studies have shown that the headpiece region is not completely disordered but contains a helix-loop-helix motif (HLH) spanning residues 9 -29 (39). To determine if this motif plays a role in degron function, we analyzed a mutant in which part of the region was deleted.…”

Section: An Idr From Chicken Fibrinogen-␣ Mimics the Degradation Funcmentioning

confidence: 99%

Cooperation between an Intrinsically Disordered Region and a Helical Segment Is Required for Ubiquitin-independent Degradation by the Proteasome

Melo¹,

Barbour

Berger

2011

Journal of Biological Chemistry

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Background: A growing number of proteins are degraded by the proteasome in a ubiquitin-independent manner. Results: Ubiquitin-independent degradation requires an intrinsically disordered region in cooperation with an ␣-helix. Conclusion: Overall conformation, rather than a specific primary sequence, underlies the function of these elements. Significance: This provides mechanistic insight into an important aspect of intracellular protein degradation.

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Refined Structure of Repressor Headpiece (1-56) Determined by Relaxation Matrix Calculations from 2D and 3D NOE Data: Change of Tertiary Structure upon Binding to the Operator

Cited by 63 publications

References 55 publications

Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling

Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling

Glycine Insertion in the Hinge Region of Lactose Repressor Protein Alters DNA Binding

Cooperation between an Intrinsically Disordered Region and a Helical Segment Is Required for Ubiquitin-independent Degradation by the Proteasome

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