Search PubMedSearch

PubMed · 4943790

Control of lambda repressor synthesis.

Abstract

Direct measurements of the intracellular level of lambda repressor have been made by a DNA-filter assay and a radioimmune assay. Transcription of cI, the structural gene for repressor, appears to initiate at two different promoters, prm and pre. Promoter pre is activated during the establishment of lysogeny by the action of cII and cIII proteins at the DNA site cY. Phage mutated in cII, cIII, or cY do not make a normal burst of repressor after infection and do not efficiently lysogenize the cell. Cro product stops repressor synthesis midway in the infective cycle. Promoter prm maintains the repressor level in established lysogens. Delection mapping places it very near the right operator (Or). Prm is activated by repressor bound to the right operator. In the absence of cII or cIII protein, repressor synthesis requires active repressor and only proceeds on genomes able to bind repressor at Or.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

L Reichardt, A D Kaiser. 1971. Control of lambda repressor synthesis.. https://doi.org/10.1073/pnas.68.9.2185

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Hyperspeckled mutants of Schizosaccharomyces pombe: frequent mating-type switching without detectable double-strand breaks.

Mating-type (MT) switching in homothallic (h90) strains of Schizosaccharomyces pombe is initiated by a DNA double-strand break (DSB) at the distal end of the expression cassette mat1. The cis-acting smt-s1 mutation C13-P11 reduces the frequency of MT switching. It is a small deletion mapping approximately 50 bp distal to the site of the DSB. From the h90 smt-s1 strain we isolated 13 mutants with a hyperspeckled iodine reaction. In these mutants the frequency of MT switching is increased. The mutations define nine different hsp genes, none of which maps in or close to the MT region. We tested one mutant of each gene for the presence of DSBs at mat1. Curiously, in none of the h90 smt-s1 hsp strains could DSBs be detected, although some sporulate nearly as efficiently as the h90 smt-n wild type. The hsp mutations show no effect in smt-0 strains; the smt-0 deletion abolishes MT switching completely. Furthermore, we tested the interaction of hsp1-1 with swi1, swi2 and swi7 mutations. hsp1-1 has no effect in swi2 strains, whereas it increases MT switching in swi7 and, to a lesser degree, in swi1 mutants.

Autoradiography

Plasma membrane fatty acid-binding protein (FABPpm) is exclusively located in the maternal facing membranes of the human placenta.

We reported earlier the presence of a 40 kDa plasma membrane fatty acid-binding protein (FABPpm) in human placenta. This protein is thought to be involved in the sequestration of unesterified free fatty acids bound to albumin from the maternal plasma for delivery to the fetus. However, its location in human placental syncytiotrophoblasts is not known. These cells are bipolar; one side facing maternal circulation (microvillous membranes), and the other side facing fetal circulation (basal membranes). Therefore, it is important to resolve the location of this protein in trophoblast membranes in order to understand fatty acid transport and metabolism in human placenta. Isolated plasma membranes vesicles were prepared respectively from the maternal facing microvillous and fetal facing surface of the human full-term placental syncytiotrophoblast. Using these membrane preparations, fatty acid binding activity, the polyacrylamide gel electrophoresis radiobinding assay for FABPpm, and Western blot analysis of FABPpm were carried out to determine the location of this protein in these membranes. Based on the above studies we conclude that the FABPpm is located exclusively in the microvillous membranes. Since FABPpm may be responsible for FFA uptake, its location in the microvillous membranes favours the unidirectional flow of maternal FFA to the fetus.

Autoradiography

Terminal deoxynucleotidil transferase is a nuclear PKC substrate.

Protein phosphorylation is the regulatory mechanism of many cellular events in response to changes in metabolic activity and environmental conditions. Seeing that PKC and TdT levels in cells are both regulated by PMA, we sought particularly intriguing to investigate TdT phosphorylation in vivo, utilizing KM-3 cells, a TdT-positive human pre-B cell line treated with PMA and in vitro, employing purified PKC and human recombinant TdT. Our data show that TdT is a substrate for PKC activity, suggesting that TdT phosphorylation could play a key role in the pathway affecting the control of gene transcription and protein synthesis during lymphoid cells differentiation.

Autoradiography