Journal of Molecular Microbiology and Biotechnology最新文献_第4页

Production of Polyhydroxyalkanoates Copolymers by Recombinant Pseudomonas in Plasmid- and Antibiotic-Free Cultures. 重组假单胞菌在质粒和无抗生素培养中生产聚羟基烷酸酯共聚物。

IF 1.2

Journal of Molecular Microbiology and Biotechnology Pub Date : 2018-01-01 Epub Date: 2019-02-19 DOI: 10.1159/000495752

Edmar Ramos Oliveira-Filho, Linda P Guamán, Thatiane Teixeira Mendonça, Paul F Long, Marilda Keico Taciro, José Gregório Cabrera Gomez, Luiziana F Silva

{"title":"Production of Polyhydroxyalkanoates Copolymers by Recombinant Pseudomonas in Plasmid- and Antibiotic-Free Cultures.","authors":"Edmar Ramos Oliveira-Filho, Linda P Guamán, Thatiane Teixeira Mendonça, Paul F Long, Marilda Keico Taciro, José Gregório Cabrera Gomez, Luiziana F Silva","doi":"10.1159/000495752","DOIUrl":"https://doi.org/10.1159/000495752","url":null,"abstract":"Three different polyhydroxyalkanoate (PHA) synthase genes (Ralstonia eutropha H16, Aeromonas sp. TSM81 or Aeromonas hydrophila ATCC7966 phaC) were introduced into the chromosome of two Pseudomonas strains: a native medium-chain-length 3-polyhydroxyalkanoate (PHAMCL) producer (Pseudomonas sp. LFM046) and a UV-induced mutant strain unable to produce PHA (Pseudomonas sp. LFM461). We reported for the first time the insertion of a chromosomal copy of phaC using the transposon system mini-Tn7. Stable antibiotic marker-free and plasmid-free recombinants were obtained. Subsequently, P(3HB-co-3HAMCL) was produced by these recombinants using glucose as the sole carbon source, without the need for co-substrates and under antibiotic-free conditions. A recombinant harboring A. hydrophila phaC produced a terpolyester composed of 84.2 mol% of 3-hydroxybutyrate, 6.3 mol% of 3-hydroxyhexanoate, and 9.5 mol% of 3-hydroxydecanoate from only glucose. Hence, we were successful in increasing the industrial potential of Pseudomonas sp. LFM461 strain by producing PHA copolymers containing 3HB and 3HAMCL using an unrelated carbon source, for the first time in a plasmid- and antibiotic-free bioprocess.","PeriodicalId":16370,"journal":{"name":"Journal of Molecular Microbiology and Biotechnology","volume":"28 5","pages":"225-235"},"PeriodicalIF":1.2,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000495752","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36981778","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 2

Expression of Cell-Penetrating Peptides Fused to Protein Cargo. 细胞穿透肽融合蛋白货物的表达。

IF 1.2

Journal of Molecular Microbiology and Biotechnology Pub Date : 2018-01-01 Epub Date: 2018-12-19 DOI: 10.1159/000494084

Sayanee Adhikari, Turki I Alahmadi, Zifan Gong, Amy J Karlsson

{"title":"Expression of Cell-Penetrating Peptides Fused to Protein Cargo.","authors":"Sayanee Adhikari, Turki I Alahmadi, Zifan Gong, Amy J Karlsson","doi":"10.1159/000494084","DOIUrl":"https://doi.org/10.1159/000494084","url":null,"abstract":"Cell-penetrating peptides (CPPs) are short peptides that can cross cell membranes. CPPs enable the delivery of biomolecules into cells and can act as drug-delivery vectors. Because recombinant production of CPPs as fusions to protein \"cargo\" leads to low yields for some CPP-cargo fusions, approaches to enhance the recombinant expression of peptide-cargo fusions need to be identified. We optimized expression conditions in Escherichia coli for fusions of CPPs (SynB, histatin-5, and MPG) to the cargo proteins biotin carboxyl carrier protein, maltose-binding protein, and green fluorescent protein. We used Western blotting to evaluate induction temperatures of 37, 30, and 20°C, and induction times of 6, 10, and 24 h. Glutathione-S-transferase was incorporated as a fusion partner to improve expression. In general, expression at 37°C for 6 and 10 h led to the highest levels of expression for the different CPP-cargo constructs. The improvements in expression of CPP-cargo fusions will allow higher yields of CPP-cargo fusions for studies of their translocation into cells.","PeriodicalId":16370,"journal":{"name":"Journal of Molecular Microbiology and Biotechnology","volume":"28 4","pages":"159-168"},"PeriodicalIF":1.2,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000494084","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36841271","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 6

Isolation and Characterization of a Lytic Bacteriophage (vB_PmiS-TH) and Its Application in Combination with Ampicillin against Planktonic and Biofilm Forms of Proteus mirabilis Isolated from Urinary Tract Infection. 水解噬菌体(vB_PmiS-TH)的分离、鉴定及其与氨苄西林联合抗尿路感染中奇异变形杆菌浮游和生物膜型的应用

IF 1.2

Journal of Molecular Microbiology and Biotechnology Pub Date : 2018-01-01 Epub Date: 2018-04-04 DOI: 10.1159/000487137

Mahsa Yazdi, Majid Bouzari, Ezzat Allah Ghaemi

{"title":"Isolation and Characterization of a Lytic Bacteriophage (vB_PmiS-TH) and Its Application in Combination with Ampicillin against Planktonic and Biofilm Forms of Proteus mirabilis Isolated from Urinary Tract Infection.","authors":"Mahsa Yazdi, Majid Bouzari, Ezzat Allah Ghaemi","doi":"10.1159/000487137","DOIUrl":"https://doi.org/10.1159/000487137","url":null,"abstract":"Proteus mirabilis is one of the most common causes of urinary tract infection (UTI), particularly in patients undergoing long-term catheterization. Phage vB_PmiS-TH was isolated from wastewater with high lytic activity against P. mirabilis (TH) isolated from UTI. The phage had rapid adsorption, a large burst size (∼260 PFU per infected cell), and high stability at a wide range of temperatures and pH values. As analyzed by transmission electron microscopy, phage vB_PmiS-TH had an icosahedral head of ∼87 × 62 nm with a noncontractile tail about 137 nm in length and 11 nm in width. It belongs to the family Siphoviridae. Combination of the phage vB_PmiS-TH with ampicillin had a higher removal activity against planktonic cells of P. mirabilis (TH) than the phage or the antibiotic alone. Combination of the phage at a multiplicity of infection of 100 with a high dose of ampicillin (246 µg/mL) showed the highest biofilm removal activity after 24 h. This study demonstrates that using a combination of phage and antibiotic could be significantly more effective against planktonic and biofilm forms of P. mirabilis (TH).","PeriodicalId":16370,"journal":{"name":"Journal of Molecular Microbiology and Biotechnology","volume":"28 1","pages":"37-46"},"PeriodicalIF":1.2,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000487137","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35977096","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 36

A Simple Method for Removal of the Chlamydomonas reinhardtii Cell Wall Using a Commercially Available Subtilisin (Alcalase). 一种利用市售枯草菌素(Alcalase)去除莱茵衣藻细胞壁的简单方法。

IF 1.2

Journal of Molecular Microbiology and Biotechnology Pub Date : 2018-01-01 Epub Date: 2018-12-19 DOI: 10.1159/000495183

Hyun-Ju Hwang, Yong Tae Kim, Nam Seon Kang, Jong Won Han

{"title":"A Simple Method for Removal of the Chlamydomonas reinhardtii Cell Wall Using a Commercially Available Subtilisin (Alcalase).","authors":"Hyun-Ju Hwang, Yong Tae Kim, Nam Seon Kang, Jong Won Han","doi":"10.1159/000495183","DOIUrl":"https://doi.org/10.1159/000495183","url":null,"abstract":"The algal cell wall is a potent barrier for delivery of transgenes for genetic engineering. Conventional methods developed for higher plant systems are often unable to penetrate or remove algal cell walls owing to their unique physical and chemical properties. Therefore, we developed a simple transformation method for Chlamydomonas reinhardtii using commercially available enzymes. Out of 7 enzymes screened for cell wall disruption, a commercial form of subtilisin (Alcalase) was the most effective at a low concentration (0.3 Anson units/mL). The efficiency was comparable to that of gamete lytic enzyme, a protease commonly used for the genetic transformation of C. reinhardtii. The transformation efficiency of our noninvasive method was similar to that of previous methods using autolysin as a cell wall-degrading enzyme in conjunction with glass bead transformation. Subtilisin showed approximately 35% sequence identity with sporangin, a hatching enzyme of C. reinhardtii, and shared conserved active domains, which may explain the effective cell wall degradation. Our trans-formation method using commercial subtilisin is more reliable and time saving than the conventional method using autolysin released from gametes for cell wall lysis.","PeriodicalId":16370,"journal":{"name":"Journal of Molecular Microbiology and Biotechnology","volume":"28 4","pages":"169-178"},"PeriodicalIF":1.2,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000495183","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36797614","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 11

Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities. 一种具有磷脂酶和酰基转移酶活性的新型热稳定性酶的鉴定

IF 1.2

Journal of Molecular Microbiology and Biotechnology Pub Date : 2018-01-01 Epub Date: 2018-08-27 DOI: 10.1159/000491698

Laura Emilce Navas, Mónica Florin-Christensen, Graciela Beatriz Benintende, Rubén Oreste Zandomeni, Marcelo Facundo Berretta

{"title":"Characterization of a Novel Thermostable Enzyme from Thermus sp. 2.9 with Phospholipase and Acyltransferase Activities.","authors":"Laura Emilce Navas, Mónica Florin-Christensen, Graciela Beatriz Benintende, Rubén Oreste Zandomeni, Marcelo Facundo Berretta","doi":"10.1159/000491698","DOIUrl":"https://doi.org/10.1159/000491698","url":null,"abstract":"Phospholipases are classified in different enzyme families according to the ester bond they cleave within phospholipids. The use of phospholipases in industrial processes has prompted the search for new enzymes with differential properties. A gene encoding a novel phospholipase (PLP_2.9) was identified in the genome of the thermophilic strain Thermus sp. 2.9. The analysis of the primary sequence unveiled a patatin-like domain. The alignment of the amino acid sequence of PLP_2.9 to other bacterial patatin-related proteins showed that the four blocks characteristic of this type of phospholipases and the amino acids representing the catalytic dyad are conserved in this protein. PLP_2.9 was overexpressed in Escherichia coli and the purified enzyme was characterized biochemically. PLP_2.9 hydrolyzed p-nitrophenyl palmitate at alkaline pH over a wide range of temperatures (55-80°C), showing high thermostability. PLP_2.9 displayed phospholipase A and acyltransferase activities on egg yolk phosphatidylcholine. Due to its high thermostability, PLP_2.9 has potential applications as a catalyst in several industrial processes.","PeriodicalId":16370,"journal":{"name":"Journal of Molecular Microbiology and Biotechnology","volume":"28 3","pages":"99-106"},"PeriodicalIF":1.2,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000491698","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36431080","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 1

Temporal and Vertical Variation in Microbial Community Composition in Response to Physicochemical Characteristics in a Water Column of Highly Eutrophied Jinhae Bay, South Korea. 晋海湾高度富营养化水体中微生物群落组成响应物理化学特征的时间和垂直变化

IF 1.2

Journal of Molecular Microbiology and Biotechnology Pub Date : 2018-01-01 Epub Date: 2018-06-29 DOI: 10.1159/000489633

Jiyoung Lee, Jae-Hyun Lim, Junhyung Park, Il-Nam Kim

{"title":"Temporal and Vertical Variation in Microbial Community Composition in Response to Physicochemical Characteristics in a Water Column of Highly Eutrophied Jinhae Bay, South Korea.","authors":"Jiyoung Lee, Jae-Hyun Lim, Junhyung Park, Il-Nam Kim","doi":"10.1159/000489633","DOIUrl":"https://doi.org/10.1159/000489633","url":null,"abstract":"Microbial communities play an essential role in marine biogeochemical cycles. Physical and biogeochemical changes in Jinhae Bay, the most anthropogenically eutrophied bay on the coasts of South Korea, are well described, but less is known about the associated changes in microbial communities. Temporal and vertical variation in microbial communities at three depths (surface, middle, and bottom) at seven time points (June to December) at the J1 sampling site were investigated on the MiSeq platform based on the 16S rRNA gene. Overall, the microbial community was dominated by Proteobacteria, Cyanobacteria, and Bacteroidetes from June to November, whereas Firmicutes were dominant in December, especially in the middle and bottom layers. The results indicate that the microbial community composition strongly varied with temporal changes in the physicochemical water properties. Moreover, the community composition differed markedly between the surface and middle layers and the bottom layer in the summer, when the water column was strongly stratified and bottom water hypoxia developed. A redundancy analysis suggested a significant correlation between physicochemical variables (i.e., temperature, salinity, and oxygen concentration) and microbial community composition. This study indicates that temporal changes in water conditions and eutrophication-induced hypoxia effectively shape the structure of the microbial community.","PeriodicalId":16370,"journal":{"name":"Journal of Molecular Microbiology and Biotechnology","volume":"28 2","pages":"65-77"},"PeriodicalIF":1.2,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000489633","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36273646","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 3

Identification of MazF Homologue in Legionella pneumophila Which Cleaves RNA at the AACU Sequence. 在AACU序列上切割RNA的嗜肺军团菌MazF同源物的鉴定。

IF 1.2

Journal of Molecular Microbiology and Biotechnology Pub Date : 2018-01-01 Epub Date: 2019-03-20 DOI: 10.1159/000497146

Mao Shaku, Jung-Ho Park, Masayori Inouye, Yoshihiro Yamaguchi

{"title":"Identification of MazF Homologue in Legionella pneumophila Which Cleaves RNA at the AACU Sequence.","authors":"Mao Shaku, Jung-Ho Park, Masayori Inouye, Yoshihiro Yamaguchi","doi":"10.1159/000497146","DOIUrl":"https://doi.org/10.1159/000497146","url":null,"abstract":"MazF is a sequence-specific endoribonuclease that is widely conserved in bacteria and archaea. Here, we found an MazF homologue (MazF-lp; LPO-p0114) in Legionella pneumophila. The mazF-lp gene overlaps 14 base pairs with the upstream gene mazE-lp (MazE-lp; LPO-p0115). The induction of mazF-lp caused cell growth arrest, while mazE-lp co-induction recovered cell growth in Escherichia coli. In vivo and in vitro primer extension experiments showed that MazF-lp is a sequence-specific endoribonuclease cleaving RNA at AACU. The endoribonuclease activity of purified MazF-lp was inhibited by purified MazE-lp. We found that MazE-lp and the MazEF-lp complex specifically bind to the palindromic sequence present in the 5'-untranslated region of the mazEF-lp operon. MazE-lp and MazEF-lp both likely function as a repressor for the mazEF-lp operon and for other genes, including icmR, whose gene product functions as a secretion chaperone for the IcmQ pore-forming protein, by specifically binding to the palindromic sequence in 5'-UTR of these genes.","PeriodicalId":16370,"journal":{"name":"Journal of Molecular Microbiology and Biotechnology","volume":"28 6","pages":"269-280"},"PeriodicalIF":1.2,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000497146","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37075326","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 4

Development and Application of a New PCR Method for Detection of Blumeria graminis f. sp. tritici. 小麦蓝灰菌PCR检测新方法的建立与应用。

IF 1.2

Journal of Molecular Microbiology and Biotechnology Pub Date : 2018-01-01 Epub Date: 2018-12-06 DOI: 10.1159/000494432

Adam Kuzdraliński, Hubert Szczerba, Anna Kot, Agnieszka Ostrowska, Michał Nowak, Marta Muszyńska

引用次数: 2

Identification of A Ring-Hydroxylating Dioxygenases Capable of Anthracene and Benz[a]anthracene Oxidization from Rhodococcus sp. P14. 红球菌P14中蒽和苯并[A]蒽氧化环羟基化双加氧酶的鉴定

IF 1.2

Journal of Molecular Microbiology and Biotechnology Pub Date : 2018-01-01 Epub Date: 2018-12-19 DOI: 10.1159/000494384

Tao Peng, An Luo, Jie Kan, Lei Liang, Tongwang Huang, Zhong Hu

{"title":"Identification of A Ring-Hydroxylating Dioxygenases Capable of Anthracene and Benz[a]anthracene Oxidization from Rhodococcus sp. P14.","authors":"Tao Peng, An Luo, Jie Kan, Lei Liang, Tongwang Huang, Zhong Hu","doi":"10.1159/000494384","DOIUrl":"https://doi.org/10.1159/000494384","url":null,"abstract":"Nowadays, contamination of soil and marine sediments by polycyclic aromatic hydrocarbons (PAHs) has become a serious problem all over the world. Rhodococcus sp. P14 was isolated from sediments with crude oil contaminate and showed degradation ability on various PAHs. The genome of Rhodococcus sp. P14 was sequenced. A gene cluster encoding a ring-hydroxylating dioxygenase Baa related to PAH degradation was identified by bioinformatics. The expression level of gene baaA was increased when P14 was cultured with anthracene, pyrene, phenanthrene, or benz[a]-anthracene as the single carbon source. The recombinant protein Baa was overexpressed in E. coli BL21 (DE3). Further investigations on the recombinant protein Baa in E. coli demonstrated that it was able to oxidize anthracene and benz [a]anthracene, resulting in 9,10-dihydroxyanthracene and 7, 12-dihydroxybenz[a]anthracene as metabolites, respectively. These results indicate that Baa plays an important role in PAH degradation in Rhodococcus sp. P14 and Baa has potential application in the bioremediation of PAHs in the contaminated environment.","PeriodicalId":16370,"journal":{"name":"Journal of Molecular Microbiology and Biotechnology","volume":"28 4","pages":"183-189"},"PeriodicalIF":1.2,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000494384","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36797615","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 19

Photoinactivation of the Staphylococcus aureus Lactose-Specific EIICB Phosphotransferase Component with p-azidophenyl-β-D-Galactoside and Phosphorylation of the Covalently Bound Substrate. 对叠氮苯基-β- d -半乳糖苷对金黄色葡萄球菌乳糖特异性EIICB磷酸转移酶组分的光失活及共价结合底物的磷酸化

IF 1.2

Journal of Molecular Microbiology and Biotechnology Pub Date : 2018-01-01 Epub Date: 2018-12-06 DOI: 10.1159/000494433

Gina Sossna-Wunder, Wolfgang Hengstenberg, Pierre Briozzo, Josef Deutscher

{"title":"Photoinactivation of the Staphylococcus aureus Lactose-Specific EIICB Phosphotransferase Component with p-azidophenyl-β-D-Galactoside and Phosphorylation of the Covalently Bound Substrate.","authors":"Gina Sossna-Wunder, Wolfgang Hengstenberg, Pierre Briozzo, Josef Deutscher","doi":"10.1159/000494433","DOIUrl":"https://doi.org/10.1159/000494433","url":null,"abstract":"Background: The phosphoenolpyruvate (PEP):lactose phosphotransferase system of Staphylococcus aureus transports and phosphorylates lactose and various phenylgalactosides. Their phosphorylation is catalyzed by the Cys476-phosphorylated EIIB domain of the lactose-specific permease enzyme IICB (EIICBLac). Phosphorylation causes the release of galactosides bound to the EIIC domain into the cytoplasm by a mechanism not yet understood.Results: Irradiation of a reaction mixture containing the photoactivatable p-azidophenyl-β-D-galactopyranoside and EIICBLac with UV light caused a loss of EIICBLac activity. Nevertheless, photoinactivated EIICBLac could still be phosphorylated with [32P]PEP. Proteolysis of photoinactivated [32P]P-EIICBLac with subtilisin provided an 11-kDa radioactive peptide. Only the sequence of its first three amino acids (-H-G-P-, position 245-247) could be determined. They are part of the substrate binding pocket in EIICs of the lactose/cellobiose PTS family. Surprisingly, while acid treatment caused hydrolysis of the phosphoryl group in active [32P]P∼EIICBLac, photoinactivated [32P]P-EIICBLac remained strongly phosphorylated.Conclusion: Phosphorylation of the -OH group at C6 of p-nitrenephenyl-β-D-galactopyranoside covalently bound to EIICLac by the histidyl-phosphorylated [32P]P∼EIIBLac domain is a likely explanation for the observed acid resistance. Placing p-nitrenephenyl-β-D-galactopyranoside into the active site of modelled EIICLac suggested that the nitrene binds to the -NH- group of Ser248, which would explain why no sequence data beyond Pro247could be obtained.","PeriodicalId":16370,"journal":{"name":"Journal of Molecular Microbiology and Biotechnology","volume":"28 3","pages":"147-158"},"PeriodicalIF":1.2,"publicationDate":"2018-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000494433","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36802002","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 3