• Title/Summary/Keyword: Relationship between compartments

Search Result 13, Processing Time 0.029 seconds

Elucidation of the Biosynthetic Pathway of Vitamin B Groups and Potential Secondary Metabolite Gene Clusters Via Genome Analysis of a Marine Bacterium Pseudoruegeria sp. M32A2M

  • Cho, Sang-Hyeok;Lee, Eunju;Ko, So-Ra;Jin, Sangrak;Song, Yoseb;Ahn, Chi-Yong;Oh, Hee-Mock;Cho, Byung-Kwan;Cho, Suhyung
    • Journal of Microbiology and Biotechnology
    • /
    • v.30 no.4
    • /
    • pp.505-514
    • /
    • 2020
  • The symbiotic nature of the relationship between algae and marine bacteria is well-studied among the complex microbial interactions. The mutual profit between algae and bacteria occurs via nutrient and vitamin exchange. It is necessary to analyze the genome sequence of a bacterium to predict its symbiotic relationships. In this study, the genome of a marine bacterium, Pseudoruegeria sp. M32A2M, isolated from the south-eastern isles (GeoJe-Do) of South Korea, was sequenced and analyzed. A draft genome (91 scaffolds) of 5.5 Mb with a DNA G+C content of 62.4% was obtained. In total, 5,101 features were identified from gene annotation, and 4,927 genes were assigned to functional proteins. We also identified transcription core proteins, RNA polymerase subunits, and sigma factors. In addition, full flagella-related gene clusters involving the flagellar body, motor, regulator, and other accessory compartments were detected even though the genus Pseudoruegeria is known to comprise non-motile bacteria. Examination of annotated KEGG pathways revealed that Pseudoruegeria sp. M32A2M has the metabolic pathways for all seven vitamin Bs, including thiamin (vitamin B1), biotin (vitamin B7), and cobalamin (vitamin B12), which are necessary for symbiosis with vitamin B auxotroph algae. We also identified gene clusters for seven secondary metabolites including ectoine, homoserine lactone, beta-lactone, terpene, lasso peptide, bacteriocin, and non-ribosomal proteins.

Changes in Aboveground Biomass and Nutrient Accumulation of the Korean-pine (Pinus koraiensis) Plantation by Stand Age at kangwondo Province (강원도(江原道) 지방(地方) 잣나무 인공림(人工林)의 임령변화(林齡變化)에 따른 지상부(地上部) 현존량(現存量)과 양분축적(養分蓄積))

  • Yi, Myong-Jong
    • Journal of Korean Society of Forest Science
    • /
    • v.87 no.2
    • /
    • pp.276-285
    • /
    • 1998
  • The aboveground biomass and nutrient content (N, P, K, Ca and Mg) of Pinus koraiensis S. et Z., aged 9, 22, 34, 46, 66 years, were measured in the Experiment Forest of Kangwon National University of Kangwondo province. The site index of the stands ranged from 13.5 to 14.2. Allometric equations (logY=alogX+b, where Y, X is ovendry mass and DBH, respectively) relating dry weights of stem, branches and needles to diameter at breast height (DBH) were developed to estimate aboveground tree biomass. Total above ground tree biomass increased with stand age from $21.8t\;ha^{-1}$ in the 9-year-old stand to $130t\;ha^{-1}$ in the 66-Year-old stand. Aboveground biomass was allocated as follows : stem> branch > foliage, except for the 9-year-old stand which had a greater proportion of foliage biomass than branch biomass. As stand age increased, an increasing proportion of annual biomass increment was allocated to stems. The aboveground biomass of shrubs and herbs ranged from 0.4 to $3.9t\;ha^{-1}$ and from 0.05 to $0.6t\;ha^{-1}$, respectively. No relationship was found between aboveground understory biomass and stand age. The mass of woody debris and forest floor varied between 0.59 to $1.54t\;ha^{-1}$ and 6.0 to $21.63t\;ha^{-1}$, respectively. Nutrient accumulation in aboveground tree biomass increased with stand age and was in the order of N > Ca > K > P > Mg. Average rates of nutrients accumulation in biomass were greatest in the early stages of stand development, and less marked as stand aged. The nutrient concentrations in different tree components decreased in the order of needle > branch > stem. There were no detectable trends in nutrient content of the forest floor and mineral soils with stand age. Understory vegetation contributed little to the nutrient pool of these Korean pine ecosystems. Mineral soil contained the Breast proportion of nutrient capital of the various ecosystem compartments.

  • PDF

The Distribution of ATPase and Porin in the Bovine Heart Mitochondrial Cristae (소(牛) 심근 미토콘드리아의 ATPase와 porin의 분포)

  • Kim, Tae-Keun;Min, Byoung-Hoon;Kim, Soo-Jin
    • Applied Microscopy
    • /
    • v.40 no.4
    • /
    • pp.261-266
    • /
    • 2010
  • ATP is the energy source synthesized at the electron transferase that consist of complex I, II, III, IV and V in mitochondrial cristae. The complex V functions as ATPase which composed of sub-complex $F_0$ and $F_1$. Porin or VDAC (voltagedependent anion-selective channel), is a family of small pore-forming proteins of the mitochondrial outer membrane, and play important roles in the regulated flux of anion, proton and metabolites between the cytosolic and mitochondrial compartments. The channel allows the diffusion of negatively charged solutes such as succinate, malate, and ATP in the fully open state, but of positively charged ions in subconducting state. In this study, in order to investigate the relationship of the function and localization between porin and ATPase we observed the distribution of porin and ATPase in the mitochondria of the bovine heart. Monoclonal antibodies against porin and ATPase ${\beta}$-subunit were used to detect porin and ATPase using light microscope with immunohistochemistry and immunofluorescence, and using electron microscope with immunogold-labeling. ATPase were stained in longitudinal section region in cardiac muscle, porin were stained in longitudinal section region in cardiac muscle. We viewed more specific pattern of localization and distribution of these proteins using immunofluorescence method. There were some region which were labeled with porin or ATPase respectively, and others which were labeled both proteins in cardiac muscle. The electron microscope results showed that immunogold labeled porin were labeled locally at mitochondrial outer membrane and ATPase were labeled evenly at mitochondrial cristae. But ATPase was not labeled at mitochondria cristae. These results confirmed the subcellular localizations of porin and ATPase in mitochondrial outer membrane and cristae. Also, we assumed that ATP synthesis always does not activation in all mitochondria exist in the bovine cardiac muscle.