Deletions within a hinge region of a specific DNA-binding protein.

Little, John W.; Hill, Sylvia A.

doi:10.1073/pnas.82.8.2301

Cited by 61 publications

(25 citation statements)

References 24 publications

(40 reference statements)

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“…While induction of lexA expression was barely affected by the presence of NTD89 following MMC addition, the induction of sosA expression was reduced from 22-fold to only 7-fold. Repressor activity of the E. coli NTD has been shown in several studies (Bertrand-Burggraf et al, 1987;Hurstel et al, 1986;Little & Hill, 1985). Neher et al (2003) further proposed that the NTD may differentially affect induction of SOS genes and our data support this notion.…”

Section: Discussionsupporting

confidence: 81%

“…In E. coli, the autocleavage occurs at Ala84-Gly85 and similar sequences are conserved in other LexA-like proteins as well as in phage repressors (Flynn et al, 2001). While autocleavage of LexA separates the two domains, the NTD is still able to bind to the SOS box and retains some LexA repressor function (BertrandBurggraf et al, 1987;Little & Hill, 1985). In fact, autocleavage of E. coli LexA exposes hidden proteolytic recognition signals promoting degradation of the CTD by the Lon protease (Little & Gellert, 1983) and the NTD by the ClpXP proteolytic complex (Neher et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

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Clp-dependent proteolysis of the LexA N-terminal domain in Staphylococcus aureus

et al. 2011

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The SOS response is governed by the transcriptional regulator LexA and is elicited in many bacterial species in response to DNA damaging conditions. Induction of the SOS response is mediated by autocleavage of the LexA repressor resulting in a C-terminal dimerization domain (CTD) and an N-terminal DNA-binding domain (NTD) known to retain some DNA-binding activity. The proteases responsible for degrading the LexA domains have been identified in Escherichia coli as ClpXP and Lon. Here, we show that in the human and animal pathogen Staphylococcus aureus, the ClpXP and ClpCP proteases contribute to degradation of the NTD and to a lesser degree the CTD. In the absence of the proteolytic subunit, ClpP, or one or both of the Clp ATPases, ClpX and ClpC, the LexA domains were stabilized after autocleavage. Production of a stabilized variant of the NTD interfered with mitomycin-mediated induction of sosA expression while leaving lexA unaffected, and also significantly reduced SOS-induced mutagenesis. Our results show that sequential proteolysis of LexA is conserved in S. aureus and that the NTD may differentially regulate a subset of genes in the SOS regulon.

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Section: Discussionsupporting

confidence: 81%

Section: Introductionmentioning

confidence: 99%

Clp-dependent proteolysis of the LexA N-terminal domain in Staphylococcus aureus

et al. 2011

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“…By comparing the migration of the two complexes with ectable much the migration of the marker proteins, we arrived at a Fig. 4C) (6,15,16,22,25,36) and for DNA-binding fingers (28).…”

mentioning

confidence: 99%

New B-lymphocyte-specific enhancer-binding protein.

Dorn¹,

Benoist²,

Mathis³

1989

Mol. Cell. Biol.

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We report the discovery of a new B-lymphocyte-specific enhancer-binding protein. A series of gel retardation assays using fragments that scan the -2172 to -1180 region of the major histocompatibility complex class II gene E. reveal a site (W) that serves as the recognition sequence for two nuclear proteins, one B-cell restricted and the other ubiquitously occurring. Certain characteristics of the NF-W1 and NF-W2 pair recall the OTF-2/ NF-A2 and OTF-1/NF-Al pair that binds to the immunoglobulin octamer, but we demonstrate that the two protein pairs are distinguishable by several criteria. NF-W1 and NF-W2 interact differentially with their common GTTGCATC binding site, display a different affinity for it, and have molecular weights that differ by about 20,000. Yet, proteolysis experiments and cross-linking analyses indicate that the two W complexes show structural relatedness.

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“…Such a type of protein structure has been demonstrated for procaryotic DNA-binding proteins: the * Corresponding author. lambda repressor CI (26,50,74), the lambda Cro protein (10,68, and references therein), the catabolite activator protein CAP (44), and the LexA protein (39).…”

mentioning

confidence: 99%

Differential protein binding in lymphocytes to a sequence in the enhancer of the mouse retrovirus SL3-3.

1988

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An electrophoretic mobility shift assay was used to characterize interactions of nuclear proteins with a DNA segment in the enhancer element of the leukemogenic murine retrovirus SL3-3. Mutation of a DNA sequence of the 5'-TGTGG-3' type decreased transcription in vivo specifically in T-lymphocyte cell lines. Extracts of nuclei from different T-lymphocyte cell lines or cells from lymphoid organs resulted in much higher amounts of complexes in vitro with this DNA sequence than did extracts from other cell lines or organs tested. Differences were also found in the sets of complexes obtained with extracts from the different types of cells. The DNA sequence specificities of the different SL3-3 enhancer factor 1 (SEFI) protein complexes were found to be distinct from those of several other previously identified DNA motifs of the TGTGG type because of differences in several nucleotides critical for binding and because these other DNA motifs could not compete with the identified DNA sequence for binding of SEF1. Limited treatment with several different proteases cleaved the SEF1 proteins such that their DNA-binding domain(s) remained and created complexes with decreased and nondistinguishable electrophoretic mobility shifts and with new properties. These results indicate that the SEF1 proteins have a structure with a flexible and relatively vulnerable hinge region linking a DNA-binding domain(s) to a more variable domain(s) with other functions. We suggest that the binding of SEFI is an essential factor for the T-cell tropism of SL3-3 and the ability of this virus to cause T-cell lymphomas.Regulatory elements, denoted enhancers, that can potentiate transcription from a variety of promoters in a relatively distance-and orientation-independent manner were originally defined in viruses and subsequently also identified for chromosomal genes (for reviews, see references 8, 19, 31, and 61). Results of competition experiments in vitro (57,62,75) and in vivo (45, 59) have shown that specific trans-acting factors are involved in enhancer function. The enhancer activity of simian virus 40 (SV40) has been shown to result from the integrated function of multiple sequence elements (79) which bind such factors (76). Results of studies of several other enhancers both in vivo and in vitro have supported the notion of a modular organization of enhancers based upon shorter sequence elements (79). Homologies between such sequence elements have also been found for enhancers with very different cell type specificities. The first noted and most commonly found homology between enhancers is an element with 5'-TGTGG-3' as its most conserved sequence feature (23,31,40,53,72,73).Enhancers have been shown to display several distinct properties that are indicative of a high degree of flexibility. (i) They can function when separated from the promoter by a long distance of DNA. (ii) They can, without displaying symmetry in their DNA sequences, function irrespective of their orientations relative to the promoter. (iii) Their sequence motifs can be re...

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Deletions within a hinge region of a specific DNA-binding protein.

Cited by 61 publications

References 24 publications

Clp-dependent proteolysis of the LexA N-terminal domain in Staphylococcus aureus

Clp-dependent proteolysis of the LexA N-terminal domain in Staphylococcus aureus

New B-lymphocyte-specific enhancer-binding protein.

Differential protein binding in lymphocytes to a sequence in the enhancer of the mouse retrovirus SL3-3.

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