Document Detail

Isolation, characterization, and postsynthetic modifications of tetrahymena high mobility group proteins.
MedLine Citation:
PMID:  6849878     Owner:  NLM     Status:  MEDLINE    
We have isolated four major high mobility group (HMG) proteins designated A, B, C, and D, together with ubiquitin from the ciliate protozoan Tetrahymena. These four HMG proteins are integral structural components of macronuclear nucleosomes. The proteins exhibit solubility properties, chromatographic behavior on carboxymethylcellulose, electrophoretic mobilities on various gel systems, and amino acid compositions similar to those of their mammalian counterparts. HMG-A is the largest, most acidic protein of the group and is phosphorylated in vivo at specific serine residues. HMG-B is both phosphorylated at serine residues and ADP ribosylated. HMG-C is not phosphorylated but is ADP ribosylated. HMG-D, the smallest, most basic protein of the group possesses an unusually high content of serine and threonine residues, and it is highly phosphorylated at both serine and threonine positions in the polypeptide chain.
B Levy-Wilson; M S Denker; E Ito
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemistry     Volume:  22     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1983 Mar 
Date Detail:
Created Date:  1983-07-08     Completed Date:  1983-07-08     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1715-21     Citation Subset:  IM    
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MeSH Terms
Adenosine Diphosphate Ribose / metabolism
Chromosomal Proteins, Non-Histone / isolation & purification*
Tetrahymena / analysis*
Reg. No./Substance:
0/Chromosomal Proteins, Non-Histone; 20762-30-5/Adenosine Diphosphate Ribose

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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