Role for RNA-binding proteins implicated in pathogenic development of Ustilago maydis
Role for RNA-binding proteins implicated in pathogenic development of Ustilago maydis
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DOI：
10.1128/ec.4.1.121-133.2005
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发表时间：
2005-01-01
期刊：
影响因子：
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通讯作者：
Feldbrügge, M
中科院分区：
文献类型：
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作者：
Becht, P;Vollmeister, E;Feldbrügge, M
玉米黑粉菌引起玉米黑穗病。成功的感染取决于许多形态转变，例如信息素依赖性接合管的形成和丝状双核生长的转变，以及宿主植物内生长过程中不同类型的菌丝结构。为了解决RNA结合蛋白在此发育过程中的参与问题，我们从编码潜在RNA结合蛋白的基因组序列中鉴定了27个开放阅读框。它们表现出与具有 Pumilio 同源结构域 (PUM)、K 同源结构域 (KHD)、双链 RNA 结合基序 (DSRM) 和 RNA 识别基序 (RRM) 的 RNA 结合蛋白的相似性。对于其中 18 个基因，我们在相容的单倍体菌株中产生了替代突变体。通过对生长行为、形态、环磷酸腺苷反应、交配和致病性的分析，我们确定了三个具有异常表型的候选者。 Khd1（一种包含三个 KHD 的 K 同源蛋白）的缺失导致了冷敏感生长表型。删除编码具有五个 KHD 的蛋白质的 khd4 会导致细胞形态异常、交配减少和毒力降低。 rrm4Delta 菌株的丝状生长和致病性受到影响。 Rrm4 是一种 RRM 蛋白，具有迄今为止独特的结构域组织，由三个 N 端 RRM 以及在聚 (A) 结合蛋白的 C 端发现的结构域组成。这些结果表明 RNA 结合蛋白在玉蜀黍形态调节和致病发展中的作用。
Ustilago maydis causes smut disease on corn. Successful infection depends on a number of morphological transitions, such as pheromone-dependent formation of conjugation tubes and the switch to filamentous dikaryotic growth, as well as different types of mycelial structures during growth within the host plant. In order to address the involvement of RNA-binding proteins during this developmental program, we identified 27 open reading frames from the genome sequence encoding potential RNA-binding proteins. They exhibit similarities to RNA-binding proteins with Pumilio homology domains (PUM), the K homology domain (KHD), the double-stranded RNA binding motif (DSRM), and the RNA recognition motif (RRM). For 18 of these genes, we generated replacement mutants in compatible haploid strains. Through analysis of growth behavior, morphology, cyclic AMP response, mating, and pathogenicity, we identified three candidates with aberrant phenotypes. Loss of Khd1, a K homology protein containing three KHDs, resulted in a cold-sensitive growth phenotype. Deletion of khd4 encoding a protein with five KHDs led to abnormal cell morphology, reduced mating, and virulence. rrm4Delta strains were affected in filamentous growth and pathogenicity. Rrm4 is an RRM protein with a so far unique domain organization consisting of three N-terminal RRMs as well as a domain found in the C terminus of poly(A)-binding proteins. These results indicate a role for RNA-binding proteins in regulation of morphology as well as in pathogenic development in U. maydis.