Cloning and biochemical analysis of β-glucoside utilization (bgl) operon without phosphotransferase system in Pectobacterium carotovorum subsp. carotovorum LY34

β-Glucosidases are widespread in bacteria and involved in the metabolism of various carbohydrate substrates. Studying of β-glucoside utilization (bgl) operons on operon of Pectobacterium carotovorum subsp. carotovorum LY34 (Pcc LY34) will help us understanding how β-glucoside utilization (bgl) opero...

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Published inMicrobiological research Vol. 167; no. 8; pp. 461 - 469
Main Authors An, Chang Long, Kim, Min Keun, Kang, Tae Ho, Kim, Jungho, Kim, Hoon, Yun, Han Dae
Format Journal Article
LanguageEnglish
Published Germany Elsevier GmbH 06.09.2012
Subjects
Amino Acid Sequence
amino acids
bacteria
Base Sequence
beta-glucosidase
bgl operon
BglK
BglY
Cloning, Molecular
DNA fragmentation
DNA, Bacterial - chemistry
DNA, Bacterial - genetics
genomic libraries
Glucosides - metabolism
magnesium
Metabolic Networks and Pathways - genetics
metabolism
Molecular Sequence Data
Open Reading Frames
Operon
Pectobacterium carotovorum - genetics
Pectobacterium carotovorum - metabolism
Pectobacterium carotovorum subsp. carotovorum
Pectobacterium carotovorum subsp. carotovorum LY34
Plant Diseases - microbiology
promoter regions
proteins
screening
sequence analysis
Sequence Analysis, DNA
Sequence Homology, Amino Acid
signal peptide
site-directed mutagenesis
sugars
terminal repeat sequences
transcription (genetics)
transportation
β-Glucosidase
β-Glucosidase
Pectobacterium carotovorum subsp. carotovorum LY34
BglK
BglY
bgl operon
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Abstract β-Glucosidases are widespread in bacteria and involved in the metabolism of various carbohydrate substrates. Studying of β-glucoside utilization (bgl) operons on operon of Pectobacterium carotovorum subsp. carotovorum LY34 (Pcc LY34) will help us understanding how β-glucoside utilization (bgl) operon can cooperate with other systems in bacterium caused soft-rot disease. Pcc LY34 causes soft-rot disease in plants and expresses multiple enzymatic forms of β-glucosidases. To fully explore the β-glucoside utilization system in Pcc LY34, we have isolated a bgl operon from a genomic library for screening of β-glucosidase activities. Sequence analysis of a 3050bp cloned DNA fragment (accession number AY870655) shows two open reading frames (bglY and bglK) that are predicted to encode proteins of 474 and 278 amino acid residues, respectively. Pair wise similarity analysis suggests BglY is a beta-glucosidase (a member of glycosyl hydrolase family 1) and BglK is a transcriptional antiterminator protein. bglY promoter region contains an inverted repeat sequence similar to transcriptional terminator. Different from other four β-glucoside utilization operons of Pcc LY34 strain, BglY contains signal peptide sequences as extracellular β-glucosidase. Comparisons of five β-glucoside utilization operons of Pcc LY34 strain showed that bglYK operon does not have phosphotransferase system domain which are responsible for sugar transportation. BglY shares 33–44% identity with other four β-glucosidases of Pcc LY34 strain. Enzyme assay showed that purified BglY enzyme hydrolyzed salicin, arbutin, pNPG, and MUG, and exhibited maximal activity at pH 7.0 and 40°C. This activity was enhanced Mg2+. Site-directed mutagenesis revealed E166 and E371 are critical of BglY's β-glucosidase activity.
AbstractList β-Glucosidases are widespread in bacteria and involved in the metabolism of various carbohydrate substrates. Studying of β-glucoside utilization (bgl) operons on operon of Pectobacterium carotovorum subsp. carotovorum LY34 (Pcc LY34) will help us understanding how β-glucoside utilization (bgl) operon can cooperate with other systems in bacterium caused soft-rot disease. Pcc LY34 causes soft-rot disease in plants and expresses multiple enzymatic forms of β-glucosidases. To fully explore the β-glucoside utilization system in Pcc LY34, we have isolated a bgl operon from a genomic library for screening of β-glucosidase activities. Sequence analysis of a 3050bp cloned DNA fragment (accession number AY870655) shows two open reading frames (bglY and bglK) that are predicted to encode proteins of 474 and 278 amino acid residues, respectively. Pair wise similarity analysis suggests BglY is a beta-glucosidase (a member of glycosyl hydrolase family 1) and BglK is a transcriptional antiterminator protein. bglY promoter region contains an inverted repeat sequence similar to transcriptional terminator. Different from other four β-glucoside utilization operons of Pcc LY34 strain, BglY contains signal peptide sequences as extracellular β-glucosidase. Comparisons of five β-glucoside utilization operons of Pcc LY34 strain showed that bglYK operon does not have phosphotransferase system domain which are responsible for sugar transportation. BglY shares 33–44% identity with other four β-glucosidases of Pcc LY34 strain. Enzyme assay showed that purified BglY enzyme hydrolyzed salicin, arbutin, pNPG, and MUG, and exhibited maximal activity at pH 7.0 and 40°C. This activity was enhanced Mg²⁺. Site-directed mutagenesis revealed E166 and E371 are critical of BglY's β-glucosidase activity.
β-Glucosidases are widespread in bacteria and involved in the metabolism of various carbohydrate substrates. Studying of β-glucoside utilization (bgl) operons on operon of Pectobacterium carotovorum subsp. carotovorum LY34 (Pcc LY34) will help us understanding how β-glucoside utilization (bgl) operon can cooperate with other systems in bacterium caused soft-rot disease. Pcc LY34 causes soft-rot disease in plants and expresses multiple enzymatic forms of β-glucosidases. To fully explore the β-glucoside utilization system in Pcc LY34, we have isolated a bgl operon from a genomic library for screening of β-glucosidase activities. Sequence analysis of a 3050bp cloned DNA fragment (accession number AY870655) shows two open reading frames (bglY and bglK) that are predicted to encode proteins of 474 and 278 amino acid residues, respectively. Pair wise similarity analysis suggests BglY is a beta-glucosidase (a member of glycosyl hydrolase family 1) and BglK is a transcriptional antiterminator protein. bglY promoter region contains an inverted repeat sequence similar to transcriptional terminator. Different from other four β-glucoside utilization operons of Pcc LY34 strain, BglY contains signal peptide sequences as extracellular β-glucosidase. Comparisons of five β-glucoside utilization operons of Pcc LY34 strain showed that bglYK operon does not have phosphotransferase system domain which are responsible for sugar transportation. BglY shares 33-44% identity with other four β-glucosidases of Pcc LY34 strain. Enzyme assay showed that purified BglY enzyme hydrolyzed salicin, arbutin, pNPG, and MUG, and exhibited maximal activity at pH 7.0 and 40°C. This activity was enhanced Mg(2+). Site-directed mutagenesis revealed E166 and E371 are critical of BglY's β-glucosidase activity.
β-Glucosidases are widespread in bacteria and involved in the metabolism of various carbohydrate substrates. Studying of β-glucoside utilization (bgl) operons on operon of Pectobacterium carotovorum subsp. carotovorum LY34 (Pcc LY34) will help us understanding how β-glucoside utilization (bgl) operon can cooperate with other systems in bacterium caused soft-rot disease. Pcc LY34 causes soft-rot disease in plants and expresses multiple enzymatic forms of β-glucosidases. To fully explore the β-glucoside utilization system in Pcc LY34, we have isolated a bgl operon from a genomic library for screening of β-glucosidase activities. Sequence analysis of a 3050bp cloned DNA fragment (accession number AY870655) shows two open reading frames (bglY and bglK) that are predicted to encode proteins of 474 and 278 amino acid residues, respectively. Pair wise similarity analysis suggests BglY is a beta-glucosidase (a member of glycosyl hydrolase family 1) and BglK is a transcriptional antiterminator protein. bglY promoter region contains an inverted repeat sequence similar to transcriptional terminator. Different from other four β-glucoside utilization operons of Pcc LY34 strain, BglY contains signal peptide sequences as extracellular β-glucosidase. Comparisons of five β-glucoside utilization operons of Pcc LY34 strain showed that bglYK operon does not have phosphotransferase system domain which are responsible for sugar transportation. BglY shares 33–44% identity with other four β-glucosidases of Pcc LY34 strain. Enzyme assay showed that purified BglY enzyme hydrolyzed salicin, arbutin, pNPG, and MUG, and exhibited maximal activity at pH 7.0 and 40°C. This activity was enhanced Mg2+. Site-directed mutagenesis revealed E166 and E371 are critical of BglY's β-glucosidase activity.
Author Kim, Hoon
An, Chang Long
Kang, Tae Ho
Yun, Han Dae
Kim, Min Keun
Kim, Jungho
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Keywords β-Glucosidase
Pectobacterium carotovorum subsp. carotovorum LY34
BglK
BglY
bgl operon
Language English
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Snippet β-Glucosidases are widespread in bacteria and involved in the metabolism of various carbohydrate substrates. Studying of β-glucoside utilization (bgl) operons...
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SubjectTerms Amino Acid Sequence
amino acids
bacteria
Base Sequence
beta-glucosidase
bgl operon
BglK
BglY
Cloning, Molecular
DNA fragmentation
DNA, Bacterial - chemistry
DNA, Bacterial - genetics
genomic libraries
Glucosides - metabolism
magnesium
Metabolic Networks and Pathways - genetics
metabolism
Molecular Sequence Data
Open Reading Frames
Operon
Pectobacterium carotovorum - genetics
Pectobacterium carotovorum - metabolism
Pectobacterium carotovorum subsp. carotovorum
Pectobacterium carotovorum subsp. carotovorum LY34
Plant Diseases - microbiology
promoter regions
proteins
screening
sequence analysis
Sequence Analysis, DNA
Sequence Homology, Amino Acid
signal peptide
site-directed mutagenesis
sugars
terminal repeat sequences
transcription (genetics)
transportation
β-Glucosidase
Title Cloning and biochemical analysis of β-glucoside utilization (bgl) operon without phosphotransferase system in Pectobacterium carotovorum subsp. carotovorum LY34
URI https://dx.doi.org/10.1016/j.micres.2012.03.004
https://www.ncbi.nlm.nih.gov/pubmed/22502871
Volume 167
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