PMID- 11856749
OWN - NLM
STAT- MEDLINE
DCOM- 20020613
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 277
IP  - 19
DP  - 2002 May 10
TI  - Comparison of the post-transcriptional regulation of the mRNAs for the surface 
      proteins PSA (GP46) and MSP (GP63) of Leishmania chagasi.
PG  - 16489-97
AB  - MSP (GP63) and PSA (GP46) are abundant 63- and 46-kDa glycolipid-anchored 
      proteins on the surface of the promastigote form of most Leishmania species. MSP 
      is a zinc metalloprotease that confers resistance to host complement-mediated 
      lysis. PSA contains internal repeats of 24 amino acids, and its function is 
      unknown. The steady state levels of mRNAs for both glycoproteins are regulated 
      post-transcriptionally, resulting in about a 30-fold increase as Leishmania 
      chagasi promastigotes grow in vitro from logarithmic phase to stationary phase. 
      Previous studies showed the 3'-untranslated regions (3'-UTRs) of these mRNAs are 
      essential for this post-transcriptional regulation. These two 3'-UTRs of 1.0 and 
      1.3 kilobases were cloned immediately downstream of a beta-galactosidase reporter 
      gene in a plasmid, and segments were systematically deleted to examine which 
      portions of the 3'-UTRs contribute to the post-transcriptional regulation. The 
      92-nucleotide segment of greatest similarity between the two 3'-UTRs was deleted 
      without loss of regulation, but the segments flanking this similarity region have 
      positive regulatory elements essential for the regulation. We propose that 
      similar, but non-identical, molecular mechanisms regulate the parallel expression 
      of these two L. chagasi mRNAs despite their lack of sequence identity. These 
      post-transcriptional mechanisms resemble the mechanism recently suggested for the 
      regulation of mRNAs encoding the dipeptide (EP) and pentapeptide (GPEET) repeat 
      proteins in Trypanosoma brucei that involves interactions between positive and 
      negative regulatory elements in the 3'-UTR.
FAU - Myung, Karen S
AU  - Myung KS
AD  - Department of Biochemistry, University of Iowa and the Veterans Affairs Medical 
      Center, Iowa City, Iowa 52242, USA.
FAU - Beetham, Jeffrey K
AU  - Beetham JK
FAU - Wilson, Mary E
AU  - Wilson ME
FAU - Donelson, John E
AU  - Donelson JE
LA  - eng
GR  - AI32135/AI/NIAID NIH HHS/United States
GR  - AI43050/AI/NIAID NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
DEP - 20020220
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (3' Untranslated Regions)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Protozoan Proteins)
RN  - 0 (RNA, Messenger)
RN  - 133655-48-8 (surface glycoprotein GP46-M-2, Leishmania)
RN  - EC 3.2.1.23 (beta-Galactosidase)
RN  - EC 3.4.24.- (Metalloendopeptidases)
RN  - EC 3.4.24.- (glycoprotein gp63, Leishmania)
SB  - IM
MH  - 3' Untranslated Regions
MH  - Animals
MH  - Base Sequence
MH  - Gene Deletion
MH  - Genes, Reporter
MH  - Leishmania/*metabolism
MH  - Membrane Glycoproteins/*metabolism
MH  - Metalloendopeptidases/*metabolism
MH  - Molecular Sequence Data
MH  - Plasmids/metabolism
MH  - Protein Binding
MH  - Protozoan Proteins/*metabolism
MH  - *RNA Processing, Post-Transcriptional
MH  - RNA, Messenger/metabolism
MH  - Transfection
MH  - beta-Galactosidase/metabolism
EDAT- 2002/02/22 10:00
MHDA- 2002/06/14 10:01
CRDT- 2002/02/22 10:00
PHST- 2002/02/22 10:00 [pubmed]
PHST- 2002/06/14 10:01 [medline]
PHST- 2002/02/22 10:00 [entrez]
AID - S0021-9258(19)60687-3 [pii]
AID - 10.1074/jbc.M200174200 [doi]
PST - ppublish
SO  - J Biol Chem. 2002 May 10;277(19):16489-97. doi: 10.1074/jbc.M200174200. Epub 2002 
      Feb 20.