Thyrotropin stimulation of the phosphorylation of serine in the N-terminal of thyroid H1 histones.
The analysis of thyroid nuclear proteins by polyacrylamide gel electrophoresis has demonstrated that thyrotropin and dibutyryl adenosine 3':5'-monophosphate stimulate specifically the phosphorylation of H1 histones in an intact cell system. This effect does not require new protein synthesis and implicates the phosphorylation of secrine residue(s) situated in the N-terminal part of H1 histones.
D000818:Animals; D002467:Cell Nucleus / Q000187:drug effects / Q000201:enzymology; D004285:Dogs; D006657:Histones / Q000378:metabolism; D066298:In Vitro Techniques; D008970:Molecular Weight; D006656:Protamine Kinase / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism*; D012694:Serine; D013961:Thyroid Gland / Q000187:drug effects / Q000201:enzymology*; D013972:Thyrotropin / Q000494:pharmacology*
D006657:Histones; D012694:Serine; D013972:Thyrotropin; D011494:Protein Kinases; D006656:Protamine Kinase