PMID- 11381136
OWN - NLM
STAT- MEDLINE
DCOM- 20010628
LR  - 20240314
IS  - 0027-8424 (Print)
IS  - 1091-6490 (Electronic)
IS  - 0027-8424 (Linking)
VI  - 98
IP  - 12
DP  - 2001 Jun 5
TI  - Localization of GAR transformylase in Escherichia coli and mammalian cells.
PG  - 6565-70
AB  - Enzymes of the de novo purine biosynthetic pathway may form a multienzyme complex 
      to facilitate substrate flux through the ten serial steps constituting the 
      pathway. One likely strategy for complex formation is the use of a structural 
      scaffold such as the cytoskeletal network or subcellular membrane of the cell to 
      mediate protein-protein interactions. To ascertain whether this strategy pertains 
      to the de novo purine enzymes, the localization pattern of the third purine 
      enzyme, glycinamide ribonucleotide transformylase (GAR Tfase) was monitored in 
      live Escherichia coli and mammalian cells. Genes encoding human as well as E. 
      coli GAR Tfase fused with green fluorescent protein (GFP) were introduced into 
      their respective cells with regulated expression of proteins and localization 
      patterns monitored by using confocal fluorescence microscopy. In both instances 
      images showed proteins to be diffused throughout the cytoplasm. Thus, GAR Tfase 
      is not localized to an existing cellular architecture, so this device is probably 
      not used to concentrate the members of the pathway. However, discrete clusters of 
      the pathway may still exist throughout the cytoplasm.
FAU - Gooljarsingh, L T
AU  - Gooljarsingh LT
AD  - Department of Chemistry, 414 Wartik Laboratory, Pennsylvania State University, 
      University Park, PA 16802, USA.
FAU - Ramcharan, J
AU  - Ramcharan J
FAU - Gilroy, S
AU  - Gilroy S
FAU - Benkovic, S J
AU  - Benkovic SJ
LA  - eng
GR  - R01 GM024129/GM/NIGMS NIH HHS/United States
GR  - R37 GM024129/GM/NIGMS NIH HHS/United States
GR  - GM 24129/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
DEP - 20010529
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  - EC 2.1.2.- (Hydroxymethyl and Formyl Transferases)
RN  - EC 2.1.2.2 (Phosphoribosylglycinamide Formyltransferase)
SB  - IM
MH  - Animals
MH  - COS Cells
MH  - Cytoplasm/enzymology
MH  - Escherichia coli/*enzymology
MH  - Humans
MH  - Hydroxymethyl and Formyl Transferases/*analysis/genetics
MH  - Microscopy, Confocal
MH  - Phosphoribosylglycinamide Formyltransferase
MH  - Transfection
PMC - PMC34393
EDAT- 2001/06/07 10:00
MHDA- 2001/06/29 10:01
PMCR- 2001/12/05
CRDT- 2001/06/07 10:00
PHST- 2001/06/07 10:00 [pubmed]
PHST- 2001/06/29 10:01 [medline]
PHST- 2001/06/07 10:00 [entrez]
PHST- 2001/12/05 00:00 [pmc-release]
AID - 121182998 [pii]
AID - 1829 [pii]
AID - 10.1073/pnas.121182998 [doi]
PST - ppublish
SO  - Proc Natl Acad Sci U S A. 2001 Jun 5;98(12):6565-70. doi: 10.1073/pnas.121182998. 
      Epub 2001 May 29.