PMID- 10559207
OWN - NLM
STAT- MEDLINE
DCOM- 19991214
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 47
DP  - 1999 Nov 19
TI  - Genomic organization of the mouse and human genes encoding the ATP
      sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2.
PG  - 33306-12
AB  - Mammalian ATP sulfurylase/adenosine 5'-phosphosulfate (APS) kinase consists of
      kinase and sulfurylase domains, and catalyzes two sequential reactions to
      synthesize the universal sulfate donor, phosphoadenosine phosphosulfate (PAPS).
      In simpler organisms, the ATP sulfurylase and APS kinase reactions are catalyzed 
      by separate enzymes encoded by two or three genes, suggesting that a fusion of
      separate genes during the course of evolution generated the bifunctional enzyme. 
      We have characterized the genomic structure of the PAPS synthetase SK2 isoform
      genes for mouse (MSK2) and human (HSK2) and analyzed the possible fusion region. 
      The MSK2 and HSK2 genes exhibit a common structure of 13 exons, including a
      15-nucleotide alternatively spliced exon 8. Enzyme activities of several
      bacterially expressed exon assemblages showed exons 1-6 encode APS kinase, while 
      exons 6-13 encode ATP sulfurylase. The MSK2 construct without the exon 6-encoded 
      peptide showed no kinase or sulfurylase activity, demonstrating that exon 6
      encodes sequences required for both activities. Exon 1 and its 5'-flanking
      sequence are highly divergent between the two species, and intron 1 of the HSK2
      gene contains a region similar to the MSK2 promoter sequence, suggesting that it 
      may be the remnant of a now-superceded regulatory region. The HSK2 promoter
      contains a GC-rich region, not present in the mouse promoter, and has few
      transcription factor binding sites in common with MSK2. These differences in the 
      two promoter regions suggest that species-specific mechanisms regulate expression
      of the SK2 isoform.
FAU - Kurima, K
AU  - Kurima K
AD  - Department of Pediatrics, University of Chicago, Chicago, Illinois 60637, USA.
FAU - Singh, B
AU  - Singh B
FAU - Schwartz, N B
AU  - Schwartz NB
LA  - eng
SI  - GENBANK/AF172857
SI  - GENBANK/AF172858
SI  - GENBANK/AF172859
SI  - GENBANK/AF172860
SI  - GENBANK/AF172861
SI  - GENBANK/AF172862
SI  - GENBANK/AF172863
SI  - GENBANK/AF172864
SI  - GENBANK/AF172865
SI  - GENBANK/AF172866
SI  - GENBANK/AF173361
SI  - GENBANK/AF173362
SI  - GENBANK/AF173363
SI  - GENBANK/AF173364
SI  - GENBANK/AF173365
GR  - AR-19622/AR/NIAMS NIH HHS/United States
GR  - HD-17332/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Multienzyme Complexes)
RN  - 0 (Recombinant Proteins)
RN  - 0 (sulfurylase kinase)
RN  - 9007-49-2 (DNA)
RN  - EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor))
RN  - EC 2.7.7.4 (Sulfate Adenylyltransferase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - DNA
MH  - *Exons
MH  - Humans
MH  - *Introns
MH  - Mice
MH  - Molecular Sequence Data
MH  - Multienzyme Complexes/*genetics
MH  - Phosphotransferases (Alcohol Group Acceptor)/*genetics
MH  - Recombinant Proteins/genetics
MH  - Sulfate Adenylyltransferase/*genetics
EDAT- 1999/11/24 00:00
MHDA- 1999/11/24 00:01
CRDT- 1999/11/24 00:00
PHST- 1999/11/24 00:00 [pubmed]
PHST- 1999/11/24 00:01 [medline]
PHST- 1999/11/24 00:00 [entrez]
AID - 10.1074/jbc.274.47.33306 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Nov 19;274(47):33306-12. doi: 10.1074/jbc.274.47.33306.