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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록· 키워드
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The HSP90 (heat shock protein 90), SGT1 (suppressor of G-two allele of Skp1), and RAR1 (required for Mia 12 resistance) proteins in plants form a molecular chaperone complex which is involved in diverse biological signaling including development and disease resistance. The three components of this complex interact via specific protein binding motifs and recruit client proteins to initiate a specific signaling cascade in response to cellular or environmental cues. Although the functions of this chaperone complex during development/growth have not been well characterized, the HSP90 chaperone and SGT1 and RAR1 co-chaperones have been demonstrated to be essential signaling components of plant immune responses. These three proteins also play important roles in activation of the mammalian Nod genes, which possess a structurally conserved plant resistance (R) protein motif, NB-LRR (nucleotide binding site-leucine rich repeat). In this review, we summarize the structures and functions of these molecular chaperones, and discuss their putative modes of action in plant immune responses.
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