Ming-Yang Ho Assistant Professor
Ph.D., Penn State University, USA
Specialty: Photosynthesis, Cyanobacteria, Microbiology
Laboratory: Life Science Building R617
(Cyanobacteria Photosynthesis Laboratory)
We welcome students/graduates who are interested in cyanobacteria or photosynthesis to join our team. You can learn techniques in Microbiology, Molecular Biology, and Biochemistry. We will also collect samples in the environment and isolate cyanobacterial strains. Feel free to send me an email for further discussion if you are interest in joining the lab.
Current Research Interests
We are studying the environmental diversity, the mechanism, and the application of cyanobacteria. We are also interested in special cyanobacteria that are thrived in extreme environments.
Research about cyanobacteria receive more and more attention in recent years. Cyanobacteria are model organisms not only for studying photosynthesis but also for industrial applications. Some cyanobacteria are rich in nutrients for dietary. In addition, valuable food additives and drugs can be isolated from some of them. By using genetic engineering, we can use cyanobacteria to produce many kinds of useful chemicals. Cyanobacteria perform photosynthesis in fixing carbon from the environment; therefore, using cyanobacteria in industrial production is friendlier to the environment than other microbes.
Far-red light (FRL, wavelength = 700-800 nm) is an important energy from the sunlight. However, few organisms can harvest FRL for oxygenic photosynthesis. The cyanobacteria studied in Ho Lab are ones of them. The goal for Ho Lab is to elucidate the mechanism in using FRL for photosynthesis. We hope one day we can transfer this system to plants, expanding their light spectrum and increasing yield.
Background: Utilization of far-red light (FRL) for oxygenic photosynthesis is an important mechanism for cyanobacteria to grow in conditions limited in visible light.
Utilization of far-red light (FRL) for oxygenic photosynthesis is important for some cyanobacteria growing in limited accessibility to visible light. Far-Red Light Photoacclimation (FaRLiP) is a photoacclimative process that transforms cyanobacteria to the status that can harvest FRL. This process includes syntheses of two FRL-absorbing chlorophylls (Chl), Chl d and Chl f, and remodeling of photosynthetic apparatus, photosystem I (PSI), photosystem II (PSII), and phycobilisome (PBS) to harvest FRL for photochemistry. The capability for performing FaRLiP comes from genes encoded in a FaRLiP gene cluster, which includes Chl f synthase, paralogous subunits of PSI, PSII, and PBS, and a phytochrome-based transcriptional regulatory cascade (the phytochrome RfpA, the downstream response regulator RfpC, and the transcriptional factor RfpB). There are at least 15 sequenced species across all five taxonomic groups in cyanobacteria are identified containing the FaRLiP gene cluster.
Figure 1. Chlorophylls d and f harvest additional wavelengths of light from sunlight.
Figure 2. The regulatory pathway of FaRLiP
(modified from Ho et al., 2017 publication number 8)
Figure 3. FaRLiP gene cluster across five taxonomic group of cyanobacteri a. (modified from Gan et al., 2014)
(Gan, F., Zhang, S., Rockwell, NC, Martin, SS, Lagarias, JC, and Bryant, DA (2014) Extensive remodeling of a cyanobacterial photosynthetic apparatus in far-red light. Science 345, 1312-1317)
Rahmatpour, N, Hauser, DA, Nelson, JM, Chen, PY, Villarreal, AJ, Ho, M -Y , and Li, FW (2021). A novel thylakoid-less isolate fills a billion-year gap in the evolution of Cyanobacteria. Curr Biol. ( link )
Tros M, Bersanini L, Shen G, Ho MY , Stokkum IHM, Bryant DA, Croce R. (2020) Harvesting far-red light: Functional integration of chlorophyll f into Photosystem I complexes of Synechococcus sp. PCC 7002. Biochim. Biophys. Acta. doi: 10.1016/j.bbabio.2020.148206 ( link )
Gisriel C, Shen G, Kurashov V, Ho MY , Zhang S, Williams D, Golbeck JH, Fromme P, Bryant DA. (2020) Structure of photosystem I acclimated to far-red light. Sci. Adv. 6, eaay6415. ( link )
Bryant DA, Shen G, Turner GM, Soulier N, Laremore TN, Ho MY . (2020) Far-red light allophycocyanin subunits play a role in chlorophyll d accumulation in far-red light. Photosynth. Res. 143 , 81-95
Ho MY , Niedzwiedzki DM, MacGregor-Chatwin C, Gerstenecker G, Hunter CN, Blankenship RE, and Bryant DA. (2019) Extensive remodeling of the photosynthetic apparatus alters energy transfer among photosynthetic complexes when cyanobacteria acclimate to far-red light. Biochim. Biophys. Acta. doi: 10.1016/j.bbabio.2019.148064
Ho MY and Bryant DA. (2019) Global transcriptional profiling of the cyanobacterium Chlorogloeopsis fritschii PCC 9212 in far-red light: insights into the regulation of chlorophyll d synthesis. Front. Microbiol. 10 , 465. doi: 10.3389/fmicb.2019.00465
Kourashov V, Ho MY , Shen G, Piedl K, Laremore TN, Bryant DA, and Golbeck JH. (2019) Energy transfer from chlorophyll f to the trapping center in naturally-occurring and engineered Photosystem I complexes. Photosynth. Res. 141 , 151-163
Shen G, Canniffe DP, Ho MY , Kurashov V, Golbeck JH, and Bryant DA. (2019) Characterization of chlorophyll f synthase heterologously produced in Synechococcus sp. PCC 7002. Photosynth. Res. 140 , 77-92
Ho MY* , Soulier NT*, Canniffe DP, Shen G, and Bryant DA. (2017) Light regulation of pigment and photosystem biosynthesis in cyanobacteria. Curr. Opin. Plant. Biol. 37 , 24-33. (*co-first author)
Ho MY , Gan F, Shen G, Zhao C, and Bryant DA. (2017) Far-red light photoacclimation (FaRLiP) in Synechococcus sp. PCC 7335: I. Regulation of FaRLiP gene expression. Photosynth. Res. 131 , 173- 186.
Ho MY , Gan F, Shen G, and Bryant DA. (2017) Far-red light photoacclimation (FaRLiP) in Synechococcus sp. PCC 7335: II. Characterization of phycobiliproteins produced during acclimation to far-red light. Photosynth. Res. 131 , 187-202.
Ho MY , Shen G, Canniffe DP, Zhao C, Bryant DA. (2016) Light-dependent chlorophyll f synthase is a highly divergent paralog of PsbA of Photosystem II. Science 353 , aaf9178.
Hung CH, Ho MY , Kanehara K, and Nakamura Y. (2013) Functional study of diacylglycerol acyltransferase type 2 family in Chlamydomonas reinhardtii. FEBS Lett. 587 , 2364-2370.