Use of Tn5tac1 to clone a pel gene encoding a highly alkaline, asparagine- rich pectate lyase isozyme from an Erwinia chrysanthemi EC16 mutant with deletions affecting the major pectate lyase isozymes

James R Alfano, Hyun Ham Jong Hyun Ham, A. Collmer

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Erwinia chrysanthemi mutant CUCPB5047, Δ(pelA pelE) Δ(pelB pelC)::28bp Δ(pelX) Δ4bp pehX::ΩCm(r), was constructed, mutated with Tn5tac1, and screened for isopropyl-β-D-thiogalactopyranoside-dependent pectate lyase (Pel) production. AKm(r) SacI fragment from the hyperexpressing Pel+ mutant CUCPB5066 was cloned into Escherichia coli and sequenced. The gene identified, pelL, encodes a novel, asparagine-rich, highly alkaline enzyme that is similar in primary structure to PelX and in enzymological properties to PelE.

Original languageEnglish (US)
Pages (from-to)4553-4556
Number of pages4
JournalJournal of bacteriology
Volume177
Issue number15
DOIs
StatePublished - Jan 1 1995

Fingerprint

Pectobacterium chrysanthemi
Asparagine
Isoenzymes
Clone Cells
Thiogalactosides
Genes
Escherichia coli
Enzymes
pectate lyase

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

Cite this

@article{d3355baeea4547fcbaa8eb34c0b24a33,
title = "Use of Tn5tac1 to clone a pel gene encoding a highly alkaline, asparagine- rich pectate lyase isozyme from an Erwinia chrysanthemi EC16 mutant with deletions affecting the major pectate lyase isozymes",
abstract = "Erwinia chrysanthemi mutant CUCPB5047, Δ(pelA pelE) Δ(pelB pelC)::28bp Δ(pelX) Δ4bp pehX::ΩCm(r), was constructed, mutated with Tn5tac1, and screened for isopropyl-β-D-thiogalactopyranoside-dependent pectate lyase (Pel) production. AKm(r) SacI fragment from the hyperexpressing Pel+ mutant CUCPB5066 was cloned into Escherichia coli and sequenced. The gene identified, pelL, encodes a novel, asparagine-rich, highly alkaline enzyme that is similar in primary structure to PelX and in enzymological properties to PelE.",
author = "Alfano, {James R} and {Jong Hyun Ham}, {Hyun Ham} and A. Collmer",
year = "1995",
month = "1",
day = "1",
doi = "10.1128/jb.177.15.4553-4556.1995",
language = "English (US)",
volume = "177",
pages = "4553--4556",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "15",

}

TY - JOUR

T1 - Use of Tn5tac1 to clone a pel gene encoding a highly alkaline, asparagine- rich pectate lyase isozyme from an Erwinia chrysanthemi EC16 mutant with deletions affecting the major pectate lyase isozymes

AU - Alfano, James R

AU - Jong Hyun Ham, Hyun Ham

AU - Collmer, A.

PY - 1995/1/1

Y1 - 1995/1/1

N2 - Erwinia chrysanthemi mutant CUCPB5047, Δ(pelA pelE) Δ(pelB pelC)::28bp Δ(pelX) Δ4bp pehX::ΩCm(r), was constructed, mutated with Tn5tac1, and screened for isopropyl-β-D-thiogalactopyranoside-dependent pectate lyase (Pel) production. AKm(r) SacI fragment from the hyperexpressing Pel+ mutant CUCPB5066 was cloned into Escherichia coli and sequenced. The gene identified, pelL, encodes a novel, asparagine-rich, highly alkaline enzyme that is similar in primary structure to PelX and in enzymological properties to PelE.

AB - Erwinia chrysanthemi mutant CUCPB5047, Δ(pelA pelE) Δ(pelB pelC)::28bp Δ(pelX) Δ4bp pehX::ΩCm(r), was constructed, mutated with Tn5tac1, and screened for isopropyl-β-D-thiogalactopyranoside-dependent pectate lyase (Pel) production. AKm(r) SacI fragment from the hyperexpressing Pel+ mutant CUCPB5066 was cloned into Escherichia coli and sequenced. The gene identified, pelL, encodes a novel, asparagine-rich, highly alkaline enzyme that is similar in primary structure to PelX and in enzymological properties to PelE.

UR - http://www.scopus.com/inward/record.url?scp=0029161161&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029161161&partnerID=8YFLogxK

U2 - 10.1128/jb.177.15.4553-4556.1995

DO - 10.1128/jb.177.15.4553-4556.1995

M3 - Article

VL - 177

SP - 4553

EP - 4556

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 15

ER -