Kinetoplastid PPEF phosphatases: dual acylated proteins expressed in the endomembrane system of Leishmania

TY - JOUR

T1 - Kinetoplastid PPEF phosphatases

T2 - dual acylated proteins expressed in the endomembrane system of Leishmania

AU - Mills, Elena

AU - Price, Helen P.

AU - Johner, Andrea

AU - Emerson, Jenny E.

AU - Smith, Deborah F.

PY - 2007/3

Y1 - 2007/3

N2 - Bioinformatic analyses have been used to identify potential downstream targets of the essential enzyme N-myristoyl transferase in the TriTryp species, Leishmania major, Trypanosoma brucei and Trypanosoma cruzi. These database searches predict similar to 60 putative N-myristoylated proteins with high confidence, including both previously characterised and novel molecules. One of the latter is an N-myristoylated protein phosphatase which has high sequence similarity to the Protein Phosphatase with EF-Hand (PPEF) proteins identified in sensory cells of higher eukaryotes. In L. major and T brucei, the PPEF-like phosphatases are encoded by single-copy genes and are constitutively expressed in all parasite life cycle stages. The N-terminus of LmPPEF is a substrate for N-myristoyl transferase and is also palmitoylated in vivo. The wild type protein has been localised to the endocytic system by immunofluorescence. The catalytic and fused C-terminal domains of the kinetoplastid and other eukaryotic PPEFs share high sequence similarity, but unlike their higher eukaryotic relatives, the C-terminal parasite EF-hand domains are degenerate and do not bind calcium. (c) 2006 Elsevier B.V. All rights reserved.

AB - Bioinformatic analyses have been used to identify potential downstream targets of the essential enzyme N-myristoyl transferase in the TriTryp species, Leishmania major, Trypanosoma brucei and Trypanosoma cruzi. These database searches predict similar to 60 putative N-myristoylated proteins with high confidence, including both previously characterised and novel molecules. One of the latter is an N-myristoylated protein phosphatase which has high sequence similarity to the Protein Phosphatase with EF-Hand (PPEF) proteins identified in sensory cells of higher eukaryotes. In L. major and T brucei, the PPEF-like phosphatases are encoded by single-copy genes and are constitutively expressed in all parasite life cycle stages. The N-terminus of LmPPEF is a substrate for N-myristoyl transferase and is also palmitoylated in vivo. The wild type protein has been localised to the endocytic system by immunofluorescence. The catalytic and fused C-terminal domains of the kinetoplastid and other eukaryotic PPEFs share high sequence similarity, but unlike their higher eukaryotic relatives, the C-terminal parasite EF-hand domains are degenerate and do not bind calcium. (c) 2006 Elsevier B.V. All rights reserved.

KW - N-myristoylation

KW - palmitoylation

KW - protein phosphatases

KW - bioinformatics

KW - DEGENERATION-C RDGC

KW - TERMINAL N-MYRISTOYLATION

KW - MOLECULAR-CLONING

KW - CATALYTIC SUBUNIT

KW - SERINE/THREONINE PHOSPHATASE

KW - PLASMODIUM-FALCIPARUM

KW - SER/THR PHOSPHATASES

KW - TRYPANOSOMA-BRUCEI

KW - ARABIDOPSIS-THALIANA

KW - AFRICAN TRYPANOSOMES

U2 - 10.1016/j.molbiopara.2006.11.008

DO - 10.1016/j.molbiopara.2006.11.008

M3 - Article

C2 - 17169445

SN - 0166-6851

VL - 152

SP - 22

EP - 34

JO - MOLECULAR AND BIOCHEMICAL PARASITOLOGY

JF - MOLECULAR AND BIOCHEMICAL PARASITOLOGY

IS - 1

ER -