Investigation of chloramphenicol acetyltransferase formation byEscherichia coli K-12 cells after changes in intracellular cyclic AMP concentration

1976 ◽  
Vol 81 (3) ◽  
pp. 338-340
Author(s):  
M. N. Boichenko ◽  
E. D. Aniskin
Keyword(s):  
Cyclic Amp ◽  
Chloramphenicol Acetyltransferase ◽  
K 12 ◽  
Byescherichia Coli

scholarly journals The cyclic AMP (cAMP)-cAMP receptor protein complex functions both as an activator and as a corepressor at the tsx-p2 promoter of Escherichia coli K-12.

1991 ◽  
Vol 173 (17) ◽  
pp. 5419-5430 ◽  
Author(s):  
P Gerlach ◽  
L Søgaard-Andersen ◽  
H Pedersen ◽  
J Martinussen ◽  
P Valentin-Hansen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cyclic Amp ◽  
Protein Complex ◽  
Receptor Protein ◽  
Camp Receptor Protein ◽  
Complex Functions ◽  
P2 Promoter ◽  
Camp Receptor ◽  
K 12

Metabolism of 12-ketooctadecanoic acid byEscherichia coli K-12 andCandida tropicalis

Lipids ◽  
1972 ◽  
Vol 7 (3) ◽  
pp. 178-181
Author(s):  
Michinao Mizugaki ◽  
Masao Sato ◽  
Mitsuru Uchiyama
Keyword(s):  
K 12 ◽  
Byescherichia Coli

Cyclic AMP and the production of sex pili by E. coli K-12 carrying derepressed sex factors

Nature ◽  
1975 ◽  
Vol 254 (5501) ◽  
pp. 628-630 ◽  
Author(s):  
C. R. HARWOOD ◽  
ELINOR MEYNELL
Keyword(s):  
Cyclic Amp ◽  
Sex Factors ◽  
E Coli ◽  
K 12

scholarly journals Impaired cyclic AMP-dependent phosphorylation renders CREB a repressor of C/EBP-induced transcription of the somatostatin gene in an insulinoma cell line.

1995 ◽  
Vol 15 (1) ◽  
pp. 415-424 ◽  
Author(s):  
M Vallejo ◽  
M E Gosse ◽  
W Beckman ◽  
J F Habener
Keyword(s):  
Transcription Factor ◽  
Cyclic Amp ◽  
Cell Line ◽  
Target Genes ◽  
Gene Promoter ◽  
Chloramphenicol Acetyltransferase ◽  
Negative Regulator ◽  
Insulinoma Cell ◽  
Insulinoma Cell Line

Transcription factor CREB regulates cyclic AMP (cAMP)-dependent gene expression by binding to and activating transcription from cAMP response elements (CREs) in the promoters of target genes. The transcriptional transactivation functions of CREB are activated by its phosphorylation by cAMP-dependent protein kinase A (PKA). In studies of many different phenotypically distinct cells, the CRE of the somatostatin gene promoter is a prototype of a highly cAMP-responsive element regulated by CREB. We now report on a somatostatin-producing rat insulinoma cell line, RIN-1027-B2, in which transcription from the somatostatin gene promoter is paradoxically repressed by CREB. We find that CREB fails to transactivate a CRE-containing somatostatin-chloramphenicol acetyltransferase reporter even when coexpressed with the catalytic subunit of PKA. CAAT box/enhancer-binding protein beta (C/EBP beta) and C/EBP-related activating transcription factor bind to the CRE in the promoter of the somatostatin gene and transactivate transcription. CREB binds competitively with C/EBP beta to the somatostatin CRE in vitro and represses C/EBP beta-induced transcription of the CRE-containing somatostatin-chloramphenicol acetyltransferase reporter. The lack of CREB-mediated transcriptional stimulation is due to the presence of a heat-stable inhibitor of PKA that prevents activation of PKA and subsequent CREB phosphorylation in the nucleus. These findings indicate that dephosphorylated CREB is a negative regulator of C/EBP-activated transcription of the somatostatin gene promoter in RIN-1027-B2 cells.

scholarly journals Accumulation of untranslated lactose-specific messenger ribonucleic acid during catabolite repression in Escherichia coli

1971 ◽  
Vol 122 (2) ◽  
pp. 219-224 ◽  
Author(s):  
M. Aboud ◽  
M. Burger
Keyword(s):  
Escherichia Coli ◽  
Carbon Source ◽  
Cyclic Amp ◽  
Direct Effect ◽  
Ribonucleic Acid ◽  
Catabolite Repression ◽  
Mrna Accumulation ◽  
Messenger Ribonucleic Acid ◽  
K 12 ◽  
Specific Mrna

When Escherichia coli K-12 Hfr.H was induced to synthesize β-galactosidase in the presence of glucose, an untranslated lactose-specific mRNA (lac-mRNA), protected from decay, was found to accumulate progressively within the cells. The lac-mRNA accumulation was unaffected by the carbon source on which the cells had been grown before the induction. The amount of the lac-mRNA available for translation was affected by catabolite repression and 3′:5′-cyclic AMP, but it remained unclear whether this was a direct effect on the formation of the lac-mRNA or a consequence of the effect on its translation.

Sign in / Sign up

Export Citation Format

Share Document