Taxonomic distribution of proteins containing Elp3 domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing Elp3 domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Metabolism of analogues of coproporphyrinogen-III with modified side chains: implications for binding at the active site of coproporphyrinogen oxidase.

Lash TD, Kaprak TA, Shen L, Jones MA
Bioorg Med Chem Lett. 2002; 12: 451-6

Porphyrinogens with modified propionate side chains bearing methyl substituents were found to be modest substrates for coproporphyrinogen oxidase; the results indicate that alteration of the substituents involved in secondary binding interactions has a comparable affect to modifying the side chain that undergoes degradation at the catalytic site.

A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme.

Wittschieben BO, Otero G, de Bizemont T, Fellows J, Erdjument-Bromage H, Ohba R, Li Y, Allis CD, Tempst P, Svejstrup JQ
Mol Cell. 1999; 4: 123-8

The elongator complex is a major component of the RNA polymerase II (RNAPII) holoenzyme responsible for transcriptional elongation in yeast. Here we identify Elp3, the 60-kilodalton subunit of elongator/RNAPII holoenzyme, as a highly conserved histone acetyltransferase (HAT) capable of acetylating core histones in vitro. In vivo, ELP3 gene deletion confers typical elp phenotypes such as slow growth adaptation, slow gene activation, and temperature sensitivity. These results suggest a role for a novel, tightly RNAPII-associated HAT in transcription of DNA packaged in chromatin.

Sequence of a P-methyltransferase-encoding gene isolated from a bialaphos-producing Streptomyces hygroscopicus.

Hidaka T, Hidaka M, Kuzuyama T, Seto H
Gene. 1995; 158: 149-50

The nucleotide sequence of the Streptomyces hygroscopicus gene encoding P-methyltransferase, catalyzing the formation of a carbon-phosphorus bond, involved in bialaphos biosynthesis, has been determined. The amino-acid sequence deduced from the nt sequence, shows homology with those of magnesium-protoporphyrin IX monomethyl ester oxidative cyclase (Mg-ProtoMe cyclase) of Rhodobacter capsulatus and the enzyme catalyzing the methylation of the aldehyde carbon of phosphonoacetaldehyde in fosfomycin biosynthesis.