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Record 1 from database: MEDLINE
Hydroxyl radical footprints and half-site arrangements of binding sites for the CysB transcriptional activator of Salmonella typhimurium.
Hryniewicz MM; Kredich NM
Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710, USA.
J Bacteriol, 1995 May, 177:9, 2343-53
CysB is a transcriptional activator for the cysteine regulon and negatively autoregulates its own gene, cysB. Transcription activation also requires an inducer, N-acetyl-L-serine. CysB is known to bind to activation sites just upstream of the -35 regions of the positively regulated cysJIH, cysK, and cysP promoters and to a repressor site centered at about +1 in the cysB promoter. Additional accessory sites have been found in positively regulated promoters. The hydroxyl radical footprinting experiments reported here indicate that the activation sites CBS-J1, CBS-K1, and CBS-P1 in the cysJIH, cysK, and cysP promoters are composed of two convergently oriented 19-bp half-sites separated by 1 or 2 bp. N-Acetyl-L-serine stimulates binding to these sites as well as to the accessory sites CBS-J2 and CBS-P2, both of which share a similar topology with activation sites. A second topology is found in the accessory site CBS-K2 and the repressor site CBS-B, which contain divergently oriented 19-bp half-sites separated by one or two helical turns. N-Acetyl-L-serine inhibits binding to these two sites. A third topology is present in the cysK and cysP promoters, where an additional half-site is oriented toward the activation site and separated from it by one helical turn. Here, CysB binds to all three half-sites, bending the DNA, and N-acetyl-L-serine decreases the extent of bending. The marked dissimilarities of these half-site arrangements and of their responses to N-acetyl-L-serine suggest that CysB, a homotetramer, binds to them with different combinations of subunits.
LA=ENG
95247666
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Bacterial Proteins|*ME; DNA-Binding Proteins|*ME; DNA, Bacterial|DE/*GE; Promoter Regions (Genetics)|DE/*GE; Salmonella typhimurium|*GE; Transcription Factors|*ME
Base Sequence; Binding Sites|DE/GE; Cysteine|BI; Gene Expression Regulation, Bacterial; Hydroxyl Radical|PD; Models, Genetic; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation|DE; Protein Binding|GE; Protein Conformation; Serine|AA/PD; Support, U.S. Gov't, P.H.S.; Transcription, Genetic
JOURNAL ARTICLE
0021-9193
UNITED STATES
0 (Bacterial Proteins); 0 (CysB protein); 0 (DNA-Binding Proteins); 0 (DNA, Bacterial); 0 (Transcription Factors); 16354-58-8 (N-acetylserine); 3352-57-6 (Hydroxyl Radical); 4371-52-2 (Cysteine); 56-45-1 (Serine)
Record 1 from database: MEDLINE
Stoichiometry of binding of CysB to the cysJIH, cysK, and cysP promoter regions of Salmonella typhimurium.
Hryniewicz MM; Kredich NM
Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710.
J Bacteriol, 1994 Jun, 176:12, 3673-82
CysB is a member of the LysR family of transcriptional activators and regulates genes of the cysteine regulon in Salmonella typhimurium and Escherichia coli. CysB binds to specific sites just upstream of the -35 regions of the cysJIH, cysK, and cysP promoters, where, in the presence of N-acetyl-L-serine, it stimulates transcription initiation. The cysK and cysP promoters contain additional binding sites, and we have proposed that CysB bends these promoters by binding to adjacent sites. N-Acetyl-L-serine is thought to decrease the magnitude of such bending. Since stoichiometric data bearing on this model have been lacking, we analyzed complexes in gel mobility shift experiments with 35S-labeled CysB and 32P-labeled promoter fragments. CysB was found to bind as a tetramer, and N-acetyl-L-serine increased the electrophoretic mobilities of one-protein complexes of the multibinding site cysK and cysP promoters without changing their stoichiometry, indicating that a single CysB tetramer can bend these promoters and that N-acetyl-L-serine diminishes such bending. Bend angles for both promoters were calculated to be 100 and 50 degrees in the absence and presence of N-acetyl-L-serine. N-Acetyl-L-serine affected neither the stoichiometry nor the electrophoretic mobility of cysJIH promoter complexes, which are not known to contain bent DNA. DNA bending may be a mechanism for sequestering CysB at certain promoter sites by increasing their affinity for this protein in the absence of N-acetyl-L-serine.
LA=ENG
94266720
Bacterial Proteins|GE/*ME/PD; DNA-Binding Proteins|*ME; Genes, Bacterial|*GE; Promoter Regions (Genetics)|*GE; Salmonella typhimurium|*GE/ME
Comparative Study; Cysteine|BI; DNA, Bacterial|CH/ME; Models, Genetic; Nucleic Acid Conformation|DE; Protein Binding; Protein Conformation; Regulon|GE; Serine|AA/PD; Support, U.S. Gov't, P.H.S.; Transcription Factors|GE; Transcription, Genetic
JOURNAL ARTICLE
0021-9193
UNITED STATES
0 (Bacterial Proteins); 0 (CysB protein); 0 (DNA-Binding Proteins); 0 (DNA, Bacterial); 0 (Transcription Factors); 16354-58-8 (N-acetylserine); 4371-52-2 (Cysteine); 56-45-1 (Serine); 87609-37-8 (LysR protein)
Record 2 from database: MEDLINE
Hydroxyl radical footprints and half-site arrangements of binding sites for the CysB transcriptional activator of Salmonella typhimurium.
Hryniewicz MM; Kredich NM
Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710, USA.
J Bacteriol, 1995 May, 177:9, 2343-53
CysB is a transcriptional activator for the cysteine regulon and negatively autoregulates its own gene, cysB. Transcription activation also requires an inducer, N-acetyl-L-serine. CysB is known to bind to activation sites just upstream of the -35 regions of the positively regulated cysJIH, cysK, and cysP promoters and to a repressor site centered at about +1 in the cysB promoter. Additional accessory sites have been found in positively regulated promoters. The hydroxyl radical footprinting experiments reported here indicate that the activation sites CBS-J1, CBS-K1, and CBS-P1 in the cysJIH, cysK, and cysP promoters are composed of two convergently oriented 19-bp half-sites separated by 1 or 2 bp. N-Acetyl-L-serine stimulates binding to these sites as well as to the accessory sites CBS-J2 and CBS-P2, both of which share a similar topology with activation sites. A second topology is found in the accessory site CBS-K2 and the repressor site CBS-B, which contain divergently oriented 19-bp half-sites separated by one or two helical turns. N-Acetyl-L-serine inhibits binding to these two sites. A third topology is present in the cysK and cysP promoters, where an additional half-site is oriented toward the activation site and separated from it by one helical turn. Here, CysB binds to all three half-sites, bending the DNA, and N-acetyl-L-serine decreases the extent of bending. The marked dissimilarities of these half-site arrangements and of their responses to N-acetyl-L-serine suggest that CysB, a homotetramer, binds to them with different combinations of subunits.
LA=ENG
95247666
Bacterial Proteins|*ME; DNA-Binding Proteins|*ME; DNA, Bacterial|DE/*GE; Promoter Regions (Genetics)|DE/*GE; Salmonella typhimurium|*GE; Transcription Factors|*ME
Base Sequence; Binding Sites|DE/GE; Cysteine|BI; Gene Expression Regulation, Bacterial; Hydroxyl Radical|PD; Models, Genetic; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation|DE; Protein Binding|GE; Protein Conformation; Serine|AA/PD; Support, U.S. Gov't, P.H.S.; Transcription, Genetic
JOURNAL ARTICLE
0021-9193
UNITED STATES
0 (Bacterial Proteins); 0 (CysB protein); 0 (DNA-Binding Proteins); 0 (DNA, Bacterial); 0 (Transcription Factors); 16354-58-8 (N-acetylserine); 3352-57-6 (Hydroxyl Radical); 4371-52-2 (Cysteine); 56-45-1 (Serine)
Record 3 from database: MEDLINE
The protease inhibitor, N-acetyl-L-leucyl-L-leucyl-leucyl-L-norleucinal, decreases the pool of major histocompatibility complex class I-binding peptides and inhibits peptide trimming in the endoplasmic reticulum.
Hughes EA; Ortmann B; Surman M; Cresswell P
Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
J Exp Med, 1996 Apr 1, 183:4, 1569-78
N-acetyl-L-leucyl-L-leucyl-L-norleucinal, (LLnL), which inhibits proteasomes in addition to other proteases, was found to prolong the association of major histocompatibility complex class I molecules with the transporters associated with antigen processing (TAP), and to slow their transport out of the endoplasmic reticulum (ER). LLnL induced a reversible accumulation of ubiquitinated proteins and changed the spectrum of peptides bound by class I molecules. These effects can probably be attributed to proteasome inhibition. Unexpectedly, in the TAP-deficient cell line .174, the rate of intracellular transport of human histocompatibility leukocyte antigen (HLA) A2 was also reduced by LLnL, and the generation of most HLA-A2-associated signal sequence peptides was inhibited. The inhibition of HLA-A2 transport in .174 cells was found to be less sensitive to LLnL than in wild-type cells, and a similar difference was found for a second protease inhibitor, benzyloxycarbonyl-L-leucyl-L-leucyl-L-phenylalanilal. These data suggest that under some conditions such inhibitors can block trimming of peptides by an ER peptidase in addition to inhibiting cytosolic peptide generation.
LA=ENG
96298952
Cysteine Proteinase Inhibitors|*PD; Endoplasmic Reticulum|*ME; Histocompatibility Antigens Class I|*ME; Leupeptins|*PD; Peptides|*ME
Amino Acid Sequence; Biological Transport; Carrier Proteins|ME; Cell Compartmentation; Cytosol|DE; Molecular Sequence Data; Oligopeptides|PD; Protein Binding; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.
JOURNAL ARTICLE
0022-1007
UNITED STATES
0 (Carrier Proteins); 0 (Cysteine Proteinase Inhibitors); 0 (Histocompatibility Antigens Class I); 0 (Leupeptins); 0 (Oligopeptides); 0 (Peptides); 110044-82-1 (acetylleucyl-leucyl-norleucinal); 143839-79-6 (N-benzyloxycarbonyl-leucyl-leucyl-phenylalaninal)
Record 4 from database: MEDLINE
Resonance energy transfer determination of the distance between the four cysteine-364 residues in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase.
Alvear M; Encinas MV; Herrera L; Cardemil E
Departamento de Ciencias QuÆimicas, Facultad de IngenierÆia y AdministraciÆon, Universidad de la Frontera, Temuco, Chile.
Arch Biochem Biophys, 1994 Mar, 309:2, 231-8
Each of the four subunits of the Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase has one cysteine residue (Cys-364) that is protected against alkylation by MnATP and that is thought to be located at (or close to) the active site (M. Alvear, M. V. Encinas, S. Latshaw, R. G. Kemp, and E. Cardemil, 1992, Biochim. Biophys. Acta 1119, 35-38). To determine the distance relationships between these residues within this tetrameric enzyme, we have derivatized one of these reactive thiols with N-acetyl-N'-(5-sulfo-1-naphthyl) ethylenediamine (AEDANS) and the others progressively with 4-[N-[(acetoxy)ethyl]-N-methylamino]-7-nitrobenz-2-oxa-1,3-diazole (ANBD). In the doubly labeled protein nonradiative singlet-singlet energy transfer between AEDANS (donor) and ANBD (acceptor) was observed. The efficiency of the energy transfer is proportional to the number of occupied acceptor sites. From these data it has been determined that one of the acceptor sites is 33 A from the donor, and the remaining two sites are 44-46 A from the donor. Cross-linking experiments revealed that mainly cross-linked dimers were produced upon reaction of the enzyme with o-phthalaldehyde and dithiobissuccinimidylpropionate. We interpret these results as an indication that this tetrameric enzyme is most likely composed of an association of two dimers.
LA=ENG
94182934
Cysteine|*CH; Energy Transfer|*; Phosphoenolpyruvate Carboxykinases|*CH; Saccharomyces cerevisiae|*EN
Amino Acid Sequence; Binding Sites; Chemistry, Physical; Cross-Linking Reagents; Fluoresceins; Fluorescent Dyes; Macromolecular Systems; Molecular Sequence Data; Naphthalenesulfonates; Oxadiazoles; Spectrometry, Fluorescence; Spectrophotometry; Sulfhydryl Reagents; Support, Non-U.S. Gov't
JOURNAL ARTICLE
0003-9861
UNITED STATES
EC 4.1.1.32 (Phosphoenolpyruvate Carboxykinases); 0 (Cross-Linking Reagents); 0 (Fluoresceins); 0 (Fluorescent Dyes); 0 (Macromolecular Systems); 0 (Naphthalenesulfonates); 0 (Oxadiazoles); 0 (Sulfhydryl Reagents); 36930-63-9 (1,5-I-AEDANS); 4371-52-2 (Cysteine); 63368-54-7 (5-iodoacetamidofluorescein); 67013-48-3 (4-(N-(iodoacetoxy)ethyl-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazole)
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