PMID- 10400623
OWN - NLM
STAT- MEDLINE
DCOM- 19990819
LR  - 20211203
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 29
DP  - 1999 Jul 16
TI  - Constitutive phosphorylation of the acidic tails of the high mobility group 1
      proteins by casein kinase II alters their conformation, stability, and DNA
      binding specificity.
PG  - 20116-22
AB  - The high mobility group (HMG) 1 and 2 proteins are the most abundant non-histone 
      components of chromosomes. Here, we report that essentially the entire pool of
      HMG1 proteins in Drosophila embryos and Chironomus cultured cells is
      phosphorylated at multiple serine residues located within acidic tails of these
      proteins. The phosphorylation sites match the consensus phosphorylation site of
      casein kinase II. Electrospray ionization mass spectroscopic analyses revealed
      that Drosophila HMGD and Chironomus HMG1a and HMG1b are double-phosphorylated and
      that Drosophila HMGZ is triple-phosphorylated. The importance of this
      post-translational modification was studied by comparing some properties of the
      native and in vitro dephosphorylated proteins. It was found that
      dephosphorylation affects the conformation of the proteins and decreases their
      conformational and metabolic stability. Moreover, it weakens binding of the
      proteins to four-way junction DNA by 2 orders of magnitude, whereas the strength 
      of binding to linear DNA remains unchanged. Based on these observations, we
      propose that the detected phosphorylation is important for the proper function
      and turnover rates of these proteins. As the occurrence of acidic tails
      containing canonical casein kinase II phosphorylation sites is common to diverse 
      HMG and other chromosomal proteins, our results are probably of general
      significance.
FAU - Wisniewski, J R
AU  - Wisniewski JR
AD  - III. Zoologisches Institut-Entwicklungsbiologie, Universitat Gottingen,
      Humboldtallee 34A, D-37073 Gottingen, Germany. jwisnie@gwdg.de
FAU - Szewczuk, Z
AU  - Szewczuk Z
FAU - Petry, I
AU  - Petry I
FAU - Schwanbeck, R
AU  - Schwanbeck R
FAU - Renner, U
AU  - Renner U
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (High Mobility Group Proteins)
RN  - 9007-49-2 (DNA)
RN  - EC 2.7.11.1 (Casein Kinase II)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
RN  - EC 3.4.- (Endopeptidases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Casein Kinase II
MH  - DNA/*metabolism
MH  - DNA-Binding Proteins/*metabolism
MH  - Drosophila/enzymology
MH  - Endopeptidases/metabolism
MH  - High Mobility Group Proteins/chemistry/*metabolism
MH  - Humans
MH  - Hydrogen-Ion Concentration
MH  - Mass Spectrometry
MH  - Molecular Sequence Data
MH  - Phosphorylation
MH  - Protein Processing, Post-Translational
MH  - Protein Serine-Threonine Kinases/*metabolism
MH  - Sequence Homology, Amino Acid
MH  - Spectrometry, Fluorescence
EDAT- 1999/07/10 00:00
MHDA- 1999/07/10 00:01
CRDT- 1999/07/10 00:00
PHST- 1999/07/10 00:00 [pubmed]
PHST- 1999/07/10 00:01 [medline]
PHST- 1999/07/10 00:00 [entrez]
AID - S0021-9258(19)72624-6 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Jul 16;274(29):20116-22.