Ser/Thr-rich repetitive motifs as targets for phosphoglycan modifications in Leishmania mexicana secreted acid phosphatase

M Wiese, T Ilg, F Lottspeich, P Overath

Research output: Contribution to journalArticle

75 Citations (Scopus)

Abstract

The insect stage of the protozoan parasite Leishmania mexicana secretes a phosphomonoesterase in the form of a filamentous complex. The polypeptide subunits of this polymer are modified by phosphoglycans and/or oligomannosyl residues linked to phosphoserine. Based on peptide sequence data of a predominant 100 kDa protein of the filamentous complex, two tandemly arranged, single copy genes, lmsap1 and lmsap2, were cloned and sequenced. lmsap1 predicts a protein with features characteristic of acid phosphatases and a remarkable serine- and threonine-rich region of 32 amino acids close to the C-terminus. In the otherwise identical lmsap2 product, this region is extended to 383 amino acids and is composed of short Ser/Thr-rich repeats. Deletion analysis demonstrates that lmsap1 encodes the major 100 kDa protein of the complex while a minor 200 kDa component is derived from the lmsap2 gene. Null mutants of either gene retain the ability to secrete acid phosphatase filaments, while a deletion of both genes results in Leishmania defective in enzyme formation. The Ser/Thr-rich domains are the targets for phosphoglycan modifications as shown by the expression of secreted fusion proteins composed of these C-terminal regions and the N-terminal domain of a lysosomal acid phosphatase.

LanguageEnglish
Pages1067-1074
Number of pages8
JournalThe EMBO journal
Volume14
Issue number6
Publication statusPublished - 15 Mar 1995

Fingerprint

Leishmania mexicana
Acid Phosphatase
Genes
Phosphoserine
Amino Acids
Peptides
Proteins
Leishmania
Gene Deletion
Threonine
Protein C
Phosphoric Monoester Hydrolases
Serine
Insects
Polymers
Parasites
Fusion reactions
Enzymes

Keywords

  • acid phosphatase
  • amino acid sequence
  • base sequence
  • carbohydrate sequence
  • cloning, molecular
  • DNA, protozoan
  • genes, protozoan
  • Leishmania mexicana
  • Lysosomes
  • molecular sequence data
  • oligosaccharides
  • protozoan proteins
  • RNA, messenger
  • RNA, protozoan
  • recombinant fusion proteins
  • repetitive sequences, nucleic acid
  • sequence alignment
  • sequence analysis, DNA
  • sequence deletion
  • serine
  • threonine

Cite this

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title = "Ser/Thr-rich repetitive motifs as targets for phosphoglycan modifications in Leishmania mexicana secreted acid phosphatase",
abstract = "The insect stage of the protozoan parasite Leishmania mexicana secretes a phosphomonoesterase in the form of a filamentous complex. The polypeptide subunits of this polymer are modified by phosphoglycans and/or oligomannosyl residues linked to phosphoserine. Based on peptide sequence data of a predominant 100 kDa protein of the filamentous complex, two tandemly arranged, single copy genes, lmsap1 and lmsap2, were cloned and sequenced. lmsap1 predicts a protein with features characteristic of acid phosphatases and a remarkable serine- and threonine-rich region of 32 amino acids close to the C-terminus. In the otherwise identical lmsap2 product, this region is extended to 383 amino acids and is composed of short Ser/Thr-rich repeats. Deletion analysis demonstrates that lmsap1 encodes the major 100 kDa protein of the complex while a minor 200 kDa component is derived from the lmsap2 gene. Null mutants of either gene retain the ability to secrete acid phosphatase filaments, while a deletion of both genes results in Leishmania defective in enzyme formation. The Ser/Thr-rich domains are the targets for phosphoglycan modifications as shown by the expression of secreted fusion proteins composed of these C-terminal regions and the N-terminal domain of a lysosomal acid phosphatase.",
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Ser/Thr-rich repetitive motifs as targets for phosphoglycan modifications in Leishmania mexicana secreted acid phosphatase. / Wiese, M; Ilg, T; Lottspeich, F; Overath, P.

In: The EMBO journal, Vol. 14, No. 6, 15.03.1995, p. 1067-1074.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Ser/Thr-rich repetitive motifs as targets for phosphoglycan modifications in Leishmania mexicana secreted acid phosphatase

AU - Wiese, M

AU - Ilg, T

AU - Lottspeich, F

AU - Overath, P

PY - 1995/3/15

Y1 - 1995/3/15

N2 - The insect stage of the protozoan parasite Leishmania mexicana secretes a phosphomonoesterase in the form of a filamentous complex. The polypeptide subunits of this polymer are modified by phosphoglycans and/or oligomannosyl residues linked to phosphoserine. Based on peptide sequence data of a predominant 100 kDa protein of the filamentous complex, two tandemly arranged, single copy genes, lmsap1 and lmsap2, were cloned and sequenced. lmsap1 predicts a protein with features characteristic of acid phosphatases and a remarkable serine- and threonine-rich region of 32 amino acids close to the C-terminus. In the otherwise identical lmsap2 product, this region is extended to 383 amino acids and is composed of short Ser/Thr-rich repeats. Deletion analysis demonstrates that lmsap1 encodes the major 100 kDa protein of the complex while a minor 200 kDa component is derived from the lmsap2 gene. Null mutants of either gene retain the ability to secrete acid phosphatase filaments, while a deletion of both genes results in Leishmania defective in enzyme formation. The Ser/Thr-rich domains are the targets for phosphoglycan modifications as shown by the expression of secreted fusion proteins composed of these C-terminal regions and the N-terminal domain of a lysosomal acid phosphatase.

AB - The insect stage of the protozoan parasite Leishmania mexicana secretes a phosphomonoesterase in the form of a filamentous complex. The polypeptide subunits of this polymer are modified by phosphoglycans and/or oligomannosyl residues linked to phosphoserine. Based on peptide sequence data of a predominant 100 kDa protein of the filamentous complex, two tandemly arranged, single copy genes, lmsap1 and lmsap2, were cloned and sequenced. lmsap1 predicts a protein with features characteristic of acid phosphatases and a remarkable serine- and threonine-rich region of 32 amino acids close to the C-terminus. In the otherwise identical lmsap2 product, this region is extended to 383 amino acids and is composed of short Ser/Thr-rich repeats. Deletion analysis demonstrates that lmsap1 encodes the major 100 kDa protein of the complex while a minor 200 kDa component is derived from the lmsap2 gene. Null mutants of either gene retain the ability to secrete acid phosphatase filaments, while a deletion of both genes results in Leishmania defective in enzyme formation. The Ser/Thr-rich domains are the targets for phosphoglycan modifications as shown by the expression of secreted fusion proteins composed of these C-terminal regions and the N-terminal domain of a lysosomal acid phosphatase.

KW - acid phosphatase

KW - amino acid sequence

KW - base sequence

KW - carbohydrate sequence

KW - cloning, molecular

KW - DNA, protozoan

KW - genes, protozoan

KW - Leishmania mexicana

KW - Lysosomes

KW - molecular sequence data

KW - oligosaccharides

KW - protozoan proteins

KW - RNA, messenger

KW - RNA, protozoan

KW - recombinant fusion proteins

KW - repetitive sequences, nucleic acid

KW - sequence alignment

KW - sequence analysis, DNA

KW - sequence deletion

KW - serine

KW - threonine

UR - http://www.ncbi.nlm.nih.gov/pmc/articles/PMC398183/

UR - http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1460-2075

M3 - Article

VL - 14

SP - 1067

EP - 1074

JO - EMBO Journal

T2 - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 6

ER -