Role of bivalent cations in the phosphoglucomutase system. IV. Study of the Mn2+ binding site by means of nuclear relaxation measurements on water protons

Biochemistry ◽  
1970 ◽  
Vol 9 (20) ◽  
pp. 3886-3894 ◽  
Author(s):  
William J. Ray ◽  
Albert S. Mildvan
Keyword(s):  
Binding Site ◽  
Nuclear Relaxation ◽  
Bivalent Cations ◽  
Relaxation Measurements

Cell-specific regulation of IRS-1 gene expression: role of E box and C/EBP binding site in HepG2 cells and CHO cells

Diabetes ◽  
1997 ◽  
Vol 46 (3) ◽  
pp. 354-362 ◽  
Author(s):  
K. Matsuda ◽  
E. Araki ◽  
R. Yoshimura ◽  
K. Tsuruzoe ◽  
N. Furukawa ◽  
...  
Keyword(s):  
Gene Expression ◽  
Binding Site ◽  
Cho Cells ◽  
Hepg2 Cells ◽  
E Box ◽  
Specific Regulation

scholarly journals Excision and transposition of Tn5 as an SOS activity in Escherichia coli.

Genetics ◽  
1991 ◽  
Vol 128 (1) ◽  
pp. 45-57 ◽  
Author(s):  
C T Kuan ◽  
S K Liu ◽  
I Tessman
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Reca Protein ◽  
Precursor Molecule ◽  
Functional Integrity ◽  
Lexa Protein ◽  
Lexa Binding ◽  
Additional Role ◽  
Stimulation Of

Abstract Excision and transposition of the Tn5 element in Escherichia coli ordinarily appear to occur by recA-independent mechanisms. However, recA(Prtc) genes, which encode RecA proteins that are constitutively activated to the protease state, greatly enhanced excision and transposition; both events appeared to occur concomitantly and without destruction of the donor DNA. The recombinase function of the RecA protein was not required. Transposition was accompanied by partial, and occasionally full, restoration of the functional integrity of the gene vacated by the excised Tn5. The stimulation of transposition was inhibited by an uncleavable LexA protein and was strongly enhanced by an additional role of the RecA(Prtc) protein besides its mediation of LexA cleavage. To account for the enhanced transposition, we suggest that (i) there may be a LexA binding site within the promoter for the IS50 transposase, (ii) activated RecA may cleave the IS50 transposition inhibitor, and (iii) the transposase may be formed by RecA cleavage of a precursor molecule.

The role of Glu196 in the environment around the substrate binding site of leucine aminopeptidase fromStreptomyces griseus

FEBS Letters ◽  
2006 ◽  
Vol 580 (3) ◽  
pp. 912-917 ◽  
Author(s):  
Jiro Arima ◽  
Yoshiko Uesugi ◽  
Misugi Uraji ◽  
Masaki Iwabuchi ◽  
Tadashi Hatanaka
Keyword(s):  
Binding Site ◽  
Leucine Aminopeptidase ◽  
Substrate Binding ◽  
Substrate Binding Site

Hybrid polymer films based ZnS nanocomposites and its optical and morphological properties: Monitoring the role of the binding-site interaction

2018 ◽  
Vol 98 ◽  
pp. 15-24 ◽  
Author(s):  
Guadalupe del C. Pizarro ◽  
Oscar G. Marambio ◽  
Manuel Jeria-Orell ◽  
Diego P. Oyarzún ◽  
Julio Sánchez
Keyword(s):  
Binding Site ◽  
Polymer Films ◽  
Morphological Properties ◽  
Hybrid Polymer

Characterization of a Specific, High Affinity [3H]Arginine8Vasopressin-Binding Site on Liver Microsomes from Different Strains of Rat and the Role of Magnesium*

Endocrinology ◽  
1986 ◽  
Vol 118 (3) ◽  
pp. 990-998 ◽  
Author(s):  
VENKAT GOPALAKRISHNAN ◽  
CHRIS R. TRIGGLE ◽  
PRAKASH V. SULAKHE ◽  
J. ROBERT McNEILL
Keyword(s):  
Binding Site ◽  
Liver Microsomes ◽  
High Affinity ◽  
Different Strains

scholarly journals Assessment of the Role of Activator Protein-1 on Transcription of the Mouse Steroidogenic Acute Regulatory Protein Gene

2004 ◽  
Vol 18 (3) ◽  
pp. 558-573 ◽  
Author(s):  
Pulak R. Manna ◽  
Darrell W. Eubank ◽  
Douglas M. Stocco
Keyword(s):  
Binding Site ◽  
Gene Transcription ◽  
Dna Sequences ◽  
Regulatory Protein ◽  
Activator Protein 1 ◽  
Transcriptional Responses ◽  
Activator Protein ◽  
Steroidogenic Acute Regulatory ◽  
Star Gene

Abstract cAMP-dependent mechanisms regulate the steroidogenic acute regulatory (StAR) protein even though its promoter lacks a consensus cAMP response-element (CRE, TGACGTCA). Transcriptional regulation of the StAR gene has been demonstrated to involve combinations of DNA sequences that provide recognition motifs for sequence-specific transcription factors. We recently identified and characterized three canonical 5′-CRE half-sites within the cAMP-responsive region (−151/−1 bp) of the mouse StAR gene. Among these CRE elements, the CRE2 half-site is analogous (TGACTGA) to an activator protein-1 (AP-1) sequence [TGA(C/G)TCA]; therefore, the role of the AP-1 transcription factor was explored in StAR gene transcription. Mutation in the AP-1 element demonstrated an approximately 50% decrease in StAR reporter activity. Using EMSA, oligonucleotide probes containing an AP-1 binding site were found to specifically bind to nuclear proteins obtained from mouse MA-10 Leydig and Y-1 adrenocortical tumor cells. The integrity of the sequence-specific AP-1 element in StAR gene transcription was assessed using the AP-1 family members, Fos (c-Fos, Fra-1, Fra-2, and Fos B) and Jun (c-Jun, Jun B, and Jun D), which demonstrated the involvement of Fos and Jun in StAR gene transcription to varying degrees. Disruption of the AP-1 binding site reversed the transcriptional responses seen with Fos and Jun. EMSA studies utilizing antibodies specific to Fos and Jun demonstrated the involvement of several AP-1 family proteins. Functional assessment of Fos and Jun was further demonstrated by transfecting antisense c-Fos, Fra-1, and dominant negative forms of Fos (A-Fos) and c-Jun (TAM-67) into MA-10 cells, which significantly (P < 0.01) repressed transcription of the StAR gene. Mutation of the AP-1 site in combination with mutations in other cis-elements resulted in a further decrease of StAR promoter activity, demonstrating a functional cooperation between these factors. Mammalian two-hybrid assays revealed high-affinity protein-protein interactions between c-Fos and c-Jun with steroidogenic factor 1, GATA-4, and CCAAT/enhancer binding protein-β. These findings demonstrate that Fos and Jun can bind to the TGACTGA element in the StAR promoter and provide novel insights into the mechanisms regulating StAR gene transcription.

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