Home LiteratureArticle Details
PMID: 2762121 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

A family of heat shock protein 70-related genes are expressed in the promastigotes of Leishmania major.

Nucleic acids research ·Vol. 17 ·No. 13 ·1989-07-11 ·Pages 5081-95

Searle S, Campos AJ, Coulson RM, Spithill TW, Smith DF

Abstract

We describe the isolation and characterisation of two novel genes of the parasitic protozoan Leishmania major that are related by nucleotide sequence homology to eukaryotic genes encoding 70 Kd. heat shock proteins. The transcription of neither gene is heat-inducible but both are constituitively-expressed throughout the promastigote stage of the parasite life cycle. A third gene shows differential expression between non-infective and infective promastigote stages in the absence of any temperature change. These genes are related by sequence homology to the tandemly-repeated hsp70 genes of trypanosomatids, but are located on different, dispersed chromosomes within the genome of L. major. The open reading frame for translation derived from one of these sequences contains a putative mitochondrial signal peptide at its amino-terminus.

MeSH Terms
Animals Base Sequence DNA/genetics,isolation & purification Genes Heat-Shock Proteins/genetics Humans Leishmania tropica/genetics Molecular Sequence Data Restriction Mapping Sequence Homology, Nucleic Acid Species Specificity Transcription, Genetic
Chemicals
Heat-Shock Proteins DNA
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Searle S
Department of Biochemistry, Imperial College of Science, Technology and Medicine, London, UK.
Campos A J
Coulson R M
Spithill T W
Smith D F
References (25)
25 references, click to expand
  1. DNA sequencing with chain-terminating inhibitors.
    Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463-7 PMID: 271968
  2. Cloning of developmentally regulated genes from Leishmania major and expression following heat induction.
    J Biol Chem. 1989 Mar 5;264(7):4244-50 PMID: 2917999
  3. pEMBL: a new family of single stranded plasmids.
    Nucleic Acids Res. 1983 Mar 25;11(6):1645-55 PMID: 6300771
  4. Identification of an infective stage of Leishmania promastigotes.
    Science. 1984 Mar 30;223(4643):1417-9 PMID: 6701528
  5. Genes of the protozoan parasite Babesia bovis that rearrange to produce RNA species with different sequences.
    Cell. 1984 Jun;37(2):653-60 PMID: 6327081
  6. "A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity". Addendum.
    Anal Biochem. 1984 Feb;137(1):266-7 PMID: 6329026
  7. Leishmanial differentiation in vitro: induction of heat shock proteins.
    Biochem Biophys Res Commun. 1984 Dec 14;125(2):755-60 PMID: 6517924
  8. Hsp70 accelerates the recovery of nucleolar morphology after heat shock.
    EMBO J. 1984 Dec 20;3(13):3095-100 PMID: 6441707
  9. Identification of cell surface carbohydrate and antigenic changes between noninfective and infective developmental stages of Leishmania major promastigotes.
    J Immunol. 1985 Jul;135(1):564-9 PMID: 2582050
  10. Induction of heat shock and stress proteins in promastigotes of three Leishmania species.
    Proc Natl Acad Sci U S A. 1985 Jul;82(13):4414-7 PMID: 3859870
  11. Heat shock genes: regulatory role for differentiation in parasitic protozoa.
    Science. 1985 Jun 21;228(4706):1443-6 PMID: 4012301
  12. Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70.
    Proc Natl Acad Sci U S A. 1985 Oct;82(19):6455-9 PMID: 3931075
  13. Uncoating ATPase is a member of the 70 kilodalton family of stress proteins.
    Cell. 1986 Apr 11;45(1):3-13 PMID: 2937542
  14. An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein.
    Cell. 1986 Jul 18;46(2):291-300 PMID: 3087629
  15. The heat-shock response.
    Annu Rev Biochem. 1986;55:1151-91 PMID: 2427013
  16. Speculations on the functions of the major heat shock and glucose-regulated proteins.
    Cell. 1986 Sep 26;46(7):959-61 PMID: 2944601
  17. Separation of large DNA molecules by contour-clamped homogeneous electric fields.
    Science. 1986 Dec 19;234(4783):1582-5 PMID: 3538420
  18. Conserved sequences and transcription of the hsp70 gene family in Trypanosoma brucei.
    Mol Cell Biol. 1986 Dec;6(12):4657-66 PMID: 3796613
  19. Genomic organization, chromosomal location and transcription of dispersed and repeated tubulin genes in Leishmania major.
    Mol Biochem Parasitol. 1987 May;24(1):23-37 PMID: 3614270
  20. Molecular karyotype of five species of Leishmania and analysis of gene locations and chromosomal rearrangements.
    Mol Biochem Parasitol. 1987 Oct;25(3):279-91 PMID: 2827021
  21. A head-to-tail tandem organization of hsp70 genes in Trypanosoma cruzi.
    Nucleic Acids Res. 1988 Feb 25;16(4):1393-406 PMID: 2831499
  22. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides.
    Nature. 1988 Apr 28;332(6167):800-5 PMID: 3282178
  23. Protein translocation across membranes.
    Science. 1988 Sep 9;241(4871):1307-13 PMID: 2842866
  24. Structure and expression of the hsp 70 gene family of Leishmania major.
    Nucleic Acids Res. 1988 Oct 25;16(20):9567-85 PMID: 3186441
  25. Trans-complementable copy-number mutants of plasmid ColE1.
    Nature. 1980 Jan 10;283(5743):216-8 PMID: 7350544
Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
Published
1989-07-11
Pages
5081-95
Language
English
Region
England
NLM ID
0411011
PMCID
PMC318096
Subset
IM
Grants
Wellcome Trust · United Kingdom
Databases
GENBANK
X14574, X14575
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com