Comparison of the post-transcriptional regulation of the mRNAs for the surface proteins PSA (GP46) and MSP (GP63) of Leishmania chagasi

Karen S Myung; Jeffrey K Beetham; Mary E Wilson; John E Donelson

doi:10.1074/jbc.M200174200

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Comparison of the post-transcriptional regulation of the mRNAs for the surface proteins PSA (GP46) and MSP (GP63) of Leishmania chagasi

Journal article

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Comparison of the post-transcriptional regulation of the mRNAs for the surface proteins PSA (GP46) and MSP (GP63) of Leishmania chagasi

Karen S Myung, Jeffrey K Beetham, Mary E Wilson and John E Donelson

The Journal of biological chemistry, Vol.277(19), pp.16489-16497

05/10/2002

DOI: 10.1074/jbc.M200174200

PMID: 11856749

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Abstract

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.

Membrane Glycoproteins - metabolism

RNA Processing, Post-Transcriptional

Molecular Sequence Data

Metalloendopeptidases - metabolism

RNA, Messenger - metabolism

Plasmids - metabolism

Animals

Protozoan Proteins - metabolism

Transfection

Base Sequence

Gene Deletion

Leishmania - metabolism

beta-Galactosidase - metabolism

Protein Binding

3' Untranslated Regions

Genes, Reporter

Details

Title: Subtitle: Comparison of the post-transcriptional regulation of the mRNAs for the surface proteins PSA (GP46) and MSP (GP63) of Leishmania chagasi
Creators: Karen S Myung - Department of Biochemistry, University of Iowa and the Veterans Affairs Medical Center, Iowa City, Iowa 52242, USA
Jeffrey K Beetham
Mary E Wilson
John E Donelson
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.277(19), pp.16489-16497
DOI: 10.1074/jbc.M200174200
PMID: 11856749
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: United States
Grant note: AI43050 / NIAID NIH HHS AI32135 / NIAID NIH HHS
Language: English
Date published: 05/10/2002
Academic Unit: Microbiology and Immunology; International Programs; Epidemiology; Biochemistry and Molecular Biology; Internal Medicine
Record Identifier: 9984001150002771

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