PMID- 10077596
OWN - NLM
STAT- MEDLINE
DCOM- 19990520
LR  - 20190501
IS  - 0027-8424 (Print)
IS  - 0027-8424 (Linking)
VI  - 96
IP  - 6
DP  - 1999 Mar 16
TI  - A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and 
      blocks cell division.
PG  - 2828-33
AB  - A new ubiquitin-processing protease (Ubp-M) has been identified in mammalian
      cells that is phosphorylated at the onset of mitosis and dephosphorylated during 
      the metaphase/anaphase transition. The carboxyl-terminal domain of this 823-aa
      protein can be phosphorylated in vitro with either extracts of mitotic cells or
      purified cdc-2/cyclin B complexes. Recombinant Ubp-M is able to deubiquitinate
      histone H2A in vitro, and the phosphorylated form is also enzymatically active.
      Wild-type Ubp-M, transiently expressed as green fluorescent protein-fusion
      proteins, localizes in the cytoplasm of cultured cells, but mutant forms, lacking
      an active-site cysteine, associate closely with mitotic chromosomes during all
      stages of cell division and remain within the nucleus during the postmitotic
      period. Cells transfected with plasmids containing mutant Ubp-M genes stop
      dividing and eventually undergo apoptosis. Ubp-M may deubiquitinate one or more
      critical proteins that are involved in the condensation of mitotic chromosomes,
      possibly acting selectively on histones H2A and H2B, the major ubiquitinated
      proteins of chromatin.
FAU - Cai, S Y
AU  - Cai SY
AD  - Boyer Center for Molecular Medicine, Yale University School of Medicine, New
      Haven, CT 06536, USA.
FAU - Babbitt, R W
AU  - Babbitt RW
FAU - Marchesi, V T
AU  - Marchesi VT
LA  - eng
SI  - GENBANK/AF126736
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Proc Natl Acad Sci U S A
JT  - Proceedings of the National Academy of Sciences of the United States of America
JID - 7505876
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (USP16 protein, human)
RN  - 0 (Ubiquitins)
RN  - EC 3.4.- (Endopeptidases)
RN  - EC 3.4.19.12 (Ubiquitin Thiolesterase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Cell Division/genetics
MH  - Endopeptidases/*genetics/metabolism
MH  - Enzyme Activation/genetics
MH  - Gene Expression Regulation, Enzymologic
MH  - HeLa Cells
MH  - Humans
MH  - Jurkat Cells
MH  - Mitosis/*genetics
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Recombinant Fusion Proteins/genetics/metabolism
MH  - Ubiquitin Thiolesterase
MH  - Ubiquitins/*metabolism
PMC - PMC15854
EDAT- 1999/03/17 00:00
MHDA- 1999/03/17 00:01
CRDT- 1999/03/17 00:00
PHST- 1999/03/17 00:00 [pubmed]
PHST- 1999/03/17 00:01 [medline]
PHST- 1999/03/17 00:00 [entrez]
AID - 10.1073/pnas.96.6.2828 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):2828-33. doi: 10.1073/pnas.96.6.2828.