Folate biosynthesis pseudogenes, ΨfolP and ΨfolK, and an O-sialoglycoprotein endopeptidase gene homolog in the phytoplasma genome

被引:22
作者
Davis, RE
Jomantiene, R
Zhao, Y
Dally, EL
机构
[1] ARS, Mol Plant Pathol Lab, USDA, Beltsville, MD 20705 USA
[2] Inst Bot, Fitovirus Lab, Microbiol Mol Biol Grp, Vilnius, Lithuania
关键词
PASTEURELLA-HAEMOLYTICA A1; MYCOPLASMALIKE ORGANISMS; DIHYDROPTEROATE SYNTHASE; CRYSTAL-STRUCTURE; PROTEIN; ACID; METALLOPROTEASES; CLASSIFICATION; IDENTIFICATION; GLYCOPROTEASE;
D O I
10.1089/104454903770946674
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Phytoplasmas are wall-less phytopathogenic prokaryotes of small genome sizes that are obligate parasites of insect vectors and plant hosts. We have cloned a clover phyllody (CPh) phytoplasma DNA locus containing five potential coding sequences. Two were identified as pseudogenes (PsifolP and PsifolK) homologous to folP and folK genes, which encode dihydropteroate synthase (DHPS) and 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK), respectively, in other bacteria. Evolution of the phytoplasma presumably involved loss of functions through the formation of these and other pseudogenes during adaptation to obligate parasitism. The findings suggest that the phytoplasma lacks capacity for de novo folate biosynthesis and possesses a transport system for absorption of preformed folate from host cells. The PsifolP-PsifolK region was flanked by three open reading frames (ORFs) encoding a DegV family protein, a hypothetical protein with a P60-like lipoprotein domain homologous with the P60-like Mycoplasma hominis protein, and a glycoprotease (Gcp) protein that possibly functions as a host adaptation or virulence factor.
引用
收藏
页码:697 / 706
页数:10
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