김옥매 교수
Ok-Mae Kim
고려대학교 생명과학과 · 생화학·유전·분자생물학
연구실 소개
김옥매 교수의 연구실은 식물의 면역 반응과 세포 내 분해 경로인 아跟토파지의 분자 기전을 중심으로 연구를 진행하고 있습니다. 특히 병원균에 의한 침입에 반응하여 세포벽에 린긴이 침착되는 과정에서 핵심적인 전사인자인 MYB15와 관련된 유전자 조절 메커니즘을 규명하고 있으며, 아uteur파지를 통해 단백질 분해와 세포 내 환경 적응을 조절하는 메커니즘을 밝혀내고 있습니다. 또한, 린긴 생합성과 아uteur파지의 상호작용을 통해 식물의 병원균 저항성과 스트레스 적응 메커니즘을 종합적으로 이해하고자 합니다.
연구 현황
연구 성과 추이
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주요 논문
13Lignin, a major component of the secondary cell wall, is important for plant growth and development. Moreover, lignin plays a pivotal role in plant innate immunity. Lignin is readily deposited upon pathogen infection and functions as a physical barrier that limits the spread of pathogens. In this study, we show that an Arabidopsis MYB transcription factor MYB15 is required for the activation of lignin biosynthesis genes such as <i>PAL</i>, <i>C4H</i>, <i>4CL</i>, <i>HCT</i>, <i>C3'H</i>, <i>COMT
The evolutionary plant-pathogen arms race has equipped plants with the immune system that can defend against pathogens. Pattern-triggered immunity and effector-triggered immunity are two major branches of innate immunity that share immune responses, including oxidative bursts, transcriptional reprogramming, and cell wall modifications such as lignin deposition. In a previous study, we reported that lignin rapidly accumulates in pathogen-infected <i>Arabidopsis</i> leaves and acts as a mechanical
Autophagy is a highly conserved processing mechanism in eukaryotes whereby cytoplasmic components are engulfed in double-membrane vesicles called autophagosomes and are delivered into organelles such as lysosomes (mammal) or vacuoles (yeast/plant) for degradation and recycling of the resulting molecules. Isolation of yeastAUTOPHAGY (ATG) genes has facilitated the identification of correspondingArabidopsis ATG genes based on sequence similarity. Genetic and molecular analyses using knockout and/o
In our previous proteomic analysis, we isolated a small GTPase RabG3b as a salicylic acid-responsive protein in Arabidopsis (Oh et al. in Plant Cell 17:2832– 2847, 2005). Here, we constructed transgenic plants overexpressing wild-type (RabG3bOX), constitutively active (RabG3bCA), and dominant negative (RabG3bDN) forms of RabG3b for functional studies. The phenotypes of these transgenic plants were indistinguishable from wild-type plants under normal growth conditions. However, both RabG3bOX and
Autophagy is a vital process that enables plants to adapt to various environmental changes. During heat stress (HS), misfolded and denatured proteins accumulate in cells, necessitating autophagy for their removal. Here, we show that a core autophagy component ATG8a is targeted for degradation via the Arg/N-degron pathway. ATG8a is expressed as two alternatively spliced transcripts encoding ATG8a isoforms, namely ATG8a(S) and ATG8a(L), with distinct N-termini. While ATG8a(S) remains stable, ATG8a
Macroautophagy/autophagy is a highly conserved catabolic pathway in eukaryotes that mediates the selective degradation and recycling of cellular components through the formation of double-membrane autophagosomes. ATG8 is a core component of autophagy and determines cargo selectivity through interactions with specific cargo receptors. Higher plants harbor multiple ATG8 isoforms, implying potential functional diversification; however, the biological significance of this isoform expansion remains l
ABSTRACT Autophagy is a vital process that enables plants to adapt to various environmental changes. During heat stress (HS), misfolded and denatured proteins accumulate in cells, necessitating autophagy for their removal. Here, we show that a core autophagy component ATG8a is targeted for degradation via the Arg/N-degron pathway. ATG8a is expressed as two alternatively spliced transcripts encoding ATG8a isoforms, namely ATG8a(S) and ATG8a(L), with distinct N-termini. While ATG8a(S) remains stab
PROTEOLYSIS1 (PRT1), an N-recognin of Arabidopsis thaliana, recognizes the N-terminal aromatic hydrophobic residue (Tyr/Phe/Trp) of its substrates and ubiquitylates them for degradation by the ubiquitin-proteasome system. Herein, we report the structures of the ZZ domain of PRT1 (PRT1ZZ) in complex with bulky hydrophobic N-degron peptides. Unlike other ZZ domains, PRT1ZZ has an unusual binding site with two hydrophobic regions. The N-terminal aromatic residues of N-degrons interact with Ile333 a
The evolutionary plant-pathogen arms race has equipped plants with the immune system that can defend against pathogens. Pattern-triggered immunity and effector-triggered immunity are two major branches of innate immunity that share immune responses, including oxidative bursts, transcriptional reprogramming, and cell wall modifications such as lignin deposition. In a previous study, we reported that lignin rapidly accumulates in pathogen-infected <i>Arabidopsis</i> leaves and acts as a mechanical
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