Searching Interacting Proteins of AtMAPRs in Arabidopsis Using Yeast Two-Hybrid Analysis

• Main Authors: Keng-Chuan Liu, 劉耿全
• Other Authors: 楊健志
• Format: Others
• Language: en_US
• Published: 2005
• Online Access: http://ndltd.ncl.edu.tw/handle/59250177352427717001

碩士 === 國立臺灣大學 === 微生物與生化學研究所 === 93 === Four AtMAPRs (AtMAPR2, AtMAPR3, AtMPAR4, and AtMAPR5) sharing 30- 40% similarity with porcine MAPR (membrane associated progesterone receptor component 1) have been identified in Arabidopsis. The function of the four AtMAPRs is not clear, but we speculated that they could participate in regulating environmental stimuli such as plant hormones, light, or stresses. Previous yeast two-hybrid assay indicated that AtMAPRs might interact with polyubiquitin, MYB3 transcription factor, AtTOC33 (GTP-binding protein), and AGT1 (alanine-glyoxylate aminotransferase). However, the presence of putative transmembrane domain of AtMAPR3, AtMAPR4, and AtMAPR5 might interfere with yeast two-hybrid results. In this work, we used truncated AtMAPR5, lacking the 1-40 amino acid residues, as bait to screen flower two-hybrid cDNA library, CD4-30. Among the 26 different interacting proteins obtained from the screening, a C3HC4-type RING protein (At3g58030) and a FKBP-type peptidyl-prolyl cis-trans isomerase, AtFKBP16-2 (At4g39710) was perhaps to function together with AtMAPR5 in Arabidopsis. We proposed two models based on these two interacting proteins that: (1) C3HC4-type RING protein might function as E3 ligase and promote the degradation of AtMAPRs. (2) AtMAPRs might be involved in electron transferring in photosynthesis with AtFKBP16-2. Further work has to be done to testify these two assumptions. Briefly, these yeast two-hybrid results provided hints to the function of AtMAPRs.