• Journal of Microbiology and Biotechnology
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• v.33 no.9
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• pp.1130-1140
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• 2023

Among the AAA+ proteases in bacteria, FtsH is a membrane-bound ATP-dependent metalloprotease, which is known to degrade many membrane proteins as well as some cytoplasmic proteins. In the intracellular pathogen Salmonella enterica serovar Typhimurium, FtsH is responsible for the proteolysis of several proteins including MgtC virulence factor and MgtA/MgtB Mg²⁺ transporters, the transcription of which is controlled by the PhoP/PhoQ two-component regulatory system. Given that PhoP response regulator itself is a cytoplasmic protein and also degraded by the cytoplasmic ClpAP protease, it seems unlikely that FtsH affects PhoP protein levels. Here we report an unexpected role of the FtsH protease protecting PhoP proteolysis from cytoplasmic ClpAP protease. In FtsH-depleted condition, PhoP protein levels decrease by ClpAP proteolysis, lowering protein levels of PhoP-controlled genes. This suggests that FtsH is required for normal activation of PhoP transcription factor. FtsH does not degrade PhoP protein but directly binds to PhoP, thus sequestering PhoP from ClpAP-mediated proteolysis. FtsH's protective effect on PhoP can be overcome by providing excess ClpP. Because PhoP is required for Salmonella's survival inside macrophages and mouse virulence, these data implicate that FtsH's sequestration of PhoP from ClpAP-mediated proteolysis is a mechanism ensuring the amount of PhoP protein during Salmonella infection.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.22 no.1
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• pp.135-166
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• 1977

Some biochemical features of varietal variation in seed protein and their implications for soybean breeding for high protein were pursued employing 86 soybean varieties of Korea, Japan, and the U.S.A. origins. Also, studied comparatively was the temporal pattern of protein components accumulation during seed development characteristic to the high protein variety. Seed protein content of the 86 soybean varieties varied 34.4 to 50.6%. Non-existence of variety having high content of both protein and oil, or high protein content with average oil content as well as high negative correlation between the content of protein and oil (r=-0.73$^{**}$) indicate strongly a great difficulty to breed high protein variety while conserving oil content. The total content of essential amino acids varied 32.82 to 36.63% and the total content of sulfur-containing amino acids varied 2.09 to 2.73% as tested for 12 varieties differing protein content from 40.0 to 50.6%. The content of methionine was positively correlated with the content of glutamic acid, which was the major amino acid (18.5%) in seed protein of soybean. In particular, the varieties Bongeui and Saikai ＃20 had high protein content as well as high content of sulfur-containing amino acids. The content of lysine was negatively correlated with that of isoleucine, but positively correlated with protein content. The content of alanine, valine or leucine was correlated positively with oil content. The seed protein of soybean was built with 12 to 16 components depending on variety as revealed on disc acrylamide gel electrophoresis. The 86 varieties were classified into 11 groups of characteristic electrophoretic pattern. The protein component of Rm=0.14(b) showed the greatest varietal variation among the components in their relative contents, and negative correlation with the content of the other components, while the protein component of Rm=0.06(a) had a significant, positive correlation with protein content. There was sequential phases of rapid decrease, slow increase and stay in the protein content during seed development. Shorter period and lower rate of decrease followed by longer period and higher rate of increase in protein content during seed development was of characteristic to high protein variety together with earlier and continuous development at higher rate of the protein component a. Considering the extremely low methionine content of the protein component a, breeding for high protein content may result in lower quality of soybean protein.n.

• Applied Biological Chemistry
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• v.10
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• pp.15-21
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• 1968

In order to fractionate the rice protein employing paper electrophoresis, 9 subjects of Korean rice and one Indica type, Pin Galw 50 were examined, the results were as follows. 1. Polished rice protein was separated into albumin, globulin, prolamine, and oryzenin. The amount of these fractions was determined by Kjeldahl method showing respectively 0.26%, 0.65%, 0.41%, and 5.01% in average. Albumin was extracted with deionized water, globulin with 10% NaCl, prolamine with 70% ethanol, and oryzenin with 0.05N-NaOH. 2. Albumin was extracted with deionized water and dialyzed by a cellophan tube. The supernatant was submitted to paper electrophoresis using phosphate buffer (pH 7.6, ${\mu}$ 0.18). Albumin was identified as monocomponent in all of 10 varieties under study. Globulin was extracted and dialyzed to remove the albumin. The precipitates were resolved in 10% saline solution and examined by paper electrophoresis. The globulin consists of two components in phosphate buffer(pH 7.6, ${\mu}$ 0.18) Any subject, regardless the origin, appears to contain globulin I and globulin II. Prolamine was extracted with 70% ethanol, dialayzed against deionized water, resolved with ethanol, and analyzed by Paper electrophoresis. It was proved as one component in the 70% alcoholic buffer(pH 9.0, ${\mu}$=0.0095). On the contrary, paper electrophoresis with oryzenin demonstrated two or three components in Sorensen's buffer(pH 13.0, ${\mu}$ 0.11). Yookoo 132, Dungpan 5, Kwansan, and Jaekun contain oryzenin I, oryzenin II, and oryzenin III. On the other hand, Paldal, Jinheung, Sukwang, Eunbangzu, Damakum, and Pin Galw 56 contain only oryzenin II, and oryzenin III. On the basis of these analyses a discussion of the differences between the protein fractions of 10 varieties was presented. 3. Globulin I varied from 0.22% to 0.46% (aver. 0.35%) in the amount, globulin II from 0.21 to 0.44%(aver. 0.32%), oryzenin I from 0.17% to 0.44%(aver. 0.3%), oryzenin II from 1.59% to 2.88%(aver. 2.23%), and oryzenin III from 2.02% to 3.57%(aver. 2.66%).

• Korean Journal of Food Science and Technology
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• v.18 no.5
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• pp.357-363
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• 1986

The thermal conductivity and thermal diffusivity of food are heavity dependent on temperature and composition. The thermal properties of pure component solids were determined by the proposed model at a temperature range of $-40^{\circ}C\;to\;150^{\circ}C$ from the experimental values of 10%, 30% and 60% solid content suspensions. The major components of food products were proteins(albumin, casein, whey protein, meat protein and gluten), lipids (milk fat, vegetable oil, lard and corn oil), carbohydrates (dextrose, lactose, sugar and starch), fibers (cellulose and pectin), all milk salts. A modified probe method was used to measure these properties of pure component suspensions of each major component of food products. General mathematical models which were developed by an optimization technique can be applied to predict the properties of food products.

• Korean Journal of Microbiology
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• v.47 no.2
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• pp.174-178
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• 2011

In Escherichia coli, DcuS/R two-component system controls fumarate import and utilization related gene expression. To understand the dynamic response of the bacterium DcuS/R two-component system with respect to fumarate concentrations, DcuS/R induced dctA promoter was integrated with GFP reporter protein. Expression monitoring study using recombinant strain showed that dctA promoter was upregulated with 1 mM of fumarate in M9 minimal medium.

• Asian Pacific Journal of Cancer Prevention
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• v.16 no.6
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• pp.2561-2567
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• 2015

Pancreatic ductal adenocarcinoma (PDAC) is a leading cause of cancer death worldwide. Our study aimed to reveal molecular mechanisms. Microarray data of GSE15471 (including 39 matching pairs of pancreatic tumor tissues and patient-matched normal tissues) was downloaded from Gene Expression Omnibus (GEO) database. We identified differentially expressed genes (DEGs) in PDAC tissues compared with normal tissues by limma package in R language. Then GO and KEGG pathway enrichment analyses were conducted with online DAVID. In addition, principal component analysis was performed and a protein-protein interaction network was constructed to study relationships between the DEGs through database STRING. A total of 532 DEGs were identified in the 38 PDAC tissues compared with 33 normal tissues. The results of principal component analysis of the top 20 DEGs could differentiate the PDAC tissues from normal tissues directly. In the PPI network, 8 of the 20 DEGs were all key genes of the collagen family. Additionally, FN1 (fibronectin 1) was also a hub node in the network. The genes of the collagen family as well as FN1 were significantly enriched in complement and coagulation cascades, ECM-receptor interaction and focal adhesion pathways. Our results suggest that genes of collagen family and FN1 may play an important role in PDAC progression. Meanwhile, these DEGs and enriched pathways, such as complement and coagulation cascades, ECM-receptor interaction and focal adhesion may be important molecular mechanisms involved in the development and progression of PDAC.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.30 no.1
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• pp.18-28
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• 1998

The main protein peak was observed in fraction No.9 and 109 when cellulase seperation was conducted by use of DEAE-Sephadex. The protein obtained from fraction No.9 has the characteristics of Cx component and that from fraction No.109 characteristics similiar to $C_1$ component. The effective reaction condition of the ensyme used was $40^{\circ}C$ in temperature. pH 5.0 and 90 minutes in treatment time. For the case of $C_1$ pH 5.5 in temperature range of $30^{\circ}C 50^^{\circ}C$, 4.0 5.5 in pH, and over 30 minutes of treatment time, the reaction was in the range of 80% of the maximum. Affinity of enzyme increased as freeness, increased, and this effect was more visible in fiber than in fines.

• The Korean Journal of Zoology
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• v.17 no.4
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• pp.159-162
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• 1974

Serum protein and hemoglobin patterns were obtained by cellulose acetate electrophoresis for several anurans. Differences were found both in the number of components from individual animal hemoglobins and in the mobility of these components. Under the conditions employed, toad and R. plancyichosenica had a single component. Other frogs showed 2-component pattern. Sera of all anurans examined contain albumin but no preablumin. Relatively few assayable proteins are found in serum from B. buro gragraizans and differ thereby from most serum patterns examined for frogs, which show complex serum protein bands. Different species have dissimilar patterns although some of bands are apparently homologous between species.

• Journal of Pharmacopuncture
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• v.9 no.2
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• pp.17-37
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• 2006

Objectives : To observe the changes in the serum proteins after intravenous injection of cultivated wild ginseng pharmacopuncture. Methods : Blood was collected before and after the administration of cultivated wild ginseng pharmacopuncture and only the serum was taken. Then differences in the spots on the scanned image after carrying out 2-Dimensional electrophoresis were located and conducted mass analysis and protein identification. Results : Following results were obtained from the comparative analysis of serum proteins before and after the administration of cultivated wild ginseng pharmacopuncture. 1. 28 spots were identified before and after the administration. 2. In confirming manifestation degree, spots with more than two-times increase were 204, 1302, 2205, 3105, 7104, 8006, spots with more than one-time increase were 1101, 1505, 2013, 2403, 3009, 3010, 4002, 4009, 6704, 8101, and spots with decrease were 205, 801, 803, 3205, 5202, 6105, 6106, 7103, 9001, 9003. 3. After conducting protein identification, proteins 205, 804, 1302, 4009, 6105, 6106 are unidentified yet, and 1l01 is unnamed protein. Protein 204 is identified as complement receptor CR2-C3d, 801 as YAPl protein, 803 as antitrypsin polymer, 1505 as PRO0684, 2013 and 3010 as proapolipoprotein, 2205 as USP48, 2403 as vitamin D binding protein, 3009 as complement component 4A preprotein, 3105 as immunoglobulin lambda chain, 3205 as transthyretin, 4002 as Ras-related protein Ral-A, 4204 as beta actin, 5202 and 7104 as apolipoprotein Ll, 6704 as alpha 2 macroglobulin precursor, 7103 as complement component 3 precursor, 8006 as testis-specific protein Y, 8101 as transferrin, 9001 as (Alpha-Oxy, Beta-(Cl12g)deoxy) T-State Human Hemoglobin, and 9003 as human hemoglobin. 4. Immune protein CR2-C3d(204), which acts against microbes and pathogenic organisms, was increased by more than two-times after the administration of pharmacopuncture. 5. Antitrypsin(803), which is secreted with inflammatory response in the lungs, was reduced after the administration of pharmacopuncture. 6. Proapolipoprotein(2013, 3010) and apolipoprotein(7104), key components of the HDL-cholesterol which plays an important role in preventing arteriosclerosis, were increased after the administration of pharmacopuncture. 7. Vitamin D binding protein(DBP, 2403), protecting the lung at the time of inflammatory response, was increased after the administration of pharmacopuncture. 8. Transthyretin(TTR, 3205), which is the main protein causing familial amyloid polyneuropathy(FAP), was decreased after the administration of pharmacopuncture. 9. Ras-related protein Ral-A(4002) that controls phospholipid metabolism, cytoskeletal formation, and membrane traffic, was increased after the administration of pharmacopuncture. 10. Testis-specific protein Y(8006), which takes part in determination of the gender, was increased by more than two-times after the administration of pharmacopuncture. 11. Transferrin(8101), which balances the iron level in the body, was increased after the administration of pharmacopuncture. Conclusion : Above results support the notion that intravenous injection of cultivated wild ginseng pharmacopuncture induce changes in serum proteins and this research can be a pioneer work in finding biomarkers.

• International Journal of Industrial Entomology and Biomaterials
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• v.21 no.2
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• pp.157-162
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• 2010

Open reading frame 35 (bm35) of the Bombyx mori nucleopolyhedrovirus (BmNPV) is a special gene whose homologues are only found in some group-I nucleopolyhedroviruses, suggesting that bm35 plays a specific role in the viral life cycle. This paper described the characterization of BmNPV bm35. Computerassisted sequence analysis shows that a putative RING finger motif is observed in the protein, Bm35 encoded by bm35. The coding sequence of bm35 was amplified and subcloned into the vector pET30a(+) and the $(His)_6$-tagged fusion protein His-Bm35 was expressed in the Escherichia coli BL21 (DE3) LysS cells. The bm35 transcript and Bm35 protein were detected in BmNPV-infected BmN cells at 12~48 h post infection (p.i.) by RT-PCR and Western blot analysis using the polyclonal antibody generated by immunizing a rabbit with purified $(His)_6$-tagged Bm35, suggesting that bm35 is synthesized in the late stage of BmNPV infection cycle. Bm35 was not a structural component associated with budded virus (BV) and occlusion derived virus (ODV). These data indicated that bm35 is a functional gene in the BmNPV life cycle.