We have developed a protein-synthesizing system reconstituted from recombinant tagged protein factors purified to homogeneity. The system was able to produce protein at a rate of about 160 μg/ml/h in a batch mode without the need for any supplementary apparatus. The protein products were easily purified within 1 h using affinity chromatography to remove the tagged protein factors. Moreover, omission of a release factor allowed efficient incorporation of an unnatural amino acid using suppressor transfer RNA (tRNA).

/pdf/cell-free-translation-reconstituted-with-purified-components-3yqtgmhg62.pdf

Cell-free translation reconstituted with purified components

https://mmbr.asm.org/content/mmbr/47/1/1.full.pdf

Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles.

The LysR family is composed of > 50 similar-sized, autoregulatory transcriptional regulators (LTTRs) that apparently evolved from a distant ancestor into subfamilies found in diverse prokaryotic genera. In response to different coinducers, LTTRs activate divergent transcription of linked target genes or unlinked regulons encoding extremely diverse functions. Mutational studies and amino acid sequence similarities of LTTRs identify: (a) a DNA-binding domain employing a helix-turn-helix motif (residues 1-65), (b) domains involved in coinducer recognition and/or response (residues 100-173 and 196-206), (c) a domain required for both DNA binding and coinducer response (residues 227-253). DNA footprinting studies suggest that in the absence of coinducer many LTTRs bind to regulated promoters via a 15-bp dyadic sequence with a common structure and position (near -65). Coinducer causes additional interactions of LTTRs with sequences near the -35 RNA polymerase binding site and/or DNA bending that results in transcription activation.

Molecular Biology of the LysR Family of Transcriptional Regulators

In this article, Axelrod applied signal transduction theory to his research on the metabolic function of serotonin, even describing
 the pineal gland as a "neurochemical transducer."

https://science.sciencemag.org/content/sci/184/4144/1341.full.pdf

The pineal gland: a neurochemical transducer.

The activity of N-acetyltransferase in the rat pineal gland is more than 15 times higher at night than during the day. This circadian rhythm persists in complete darkness, or in blinded animals, and is suppressed in constant lighting. The N-acetyltransferase rhythm is 180 degrees out of phase with the serotonin rhythm and is similar to the norepinephrine and melatonin rhythms. Experiments in vitro indicate that norepinephrine, not serotonin, regulates the activity of N-acetyl-transferase through a highly specific receptor.

https://science.sciencemag.org/content/sci/169/3950/1093.full.pdf

Betty Redfield

Papers

Biosynthesis of melatonin: enzymic conversion of serotonin to N-acetylserotonin.

Studies with reversible inhibitors of monoamine oxidase: Harmaline and related compounds

Studies on the terminal reaction in the biosynthesis of methionine.

Methionyl soluble ribonucleic acid transformylase. I. Purification and partial characterization.

Soluble monoamine oxidase; its properties and actions on serotonin