Composition and synthesis during G1 and S phase of a high mobility group-E/G component from Chinese hamster ovary cells.
A perchloric acid soluble protein from the sedimented chromatin of blended Chinese hamster ovary (line CHO) cells has been isolated by guanidine hydrochloride gradient chromatography on Bio . Rex-70 ion exchange resin. The amino acid composition of the protein (designated as CHO HMG-E/G) is similar to that of mouse HMG-E, but it differs from that of bovine HMG-14 and HMG-17 or any possible mixture of the two. CHO HMG-E/G incorporates [32P]phosphate like HMG-14 and HMG-17 class proteins from other species, but all resolvable molecular species incorporate phosphate, and the more highly-phosphorylated band migrates faster, rather than slower, than the other in acid-urea gel systems. Incorporation of [3H]lysine into HMG-E/G following release from isoleucine deprivation G1 block indicates that the protein is extensively synthesized during both the G1 and S phases of the cell cycle.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002453:Cell Cycle; D002460:Cell Line; D002868:Chromosomal Proteins, Non-Histone / Q000235:genetics* / Q000302:isolation & purification; D006224:Cricetinae; D003412:Cricetulus; D005260:Female; D006609:High Mobility Group Proteins; D007399:Interphase; D007700:Kinetics; D008970:Molecular Weight; D010053:Ovary; D010766:Phosphorylation
D000596:Amino Acids; D002868:Chromosomal Proteins, Non-Histone; D006609:High Mobility Group Proteins