Characterization of the genes encoding integrative and excisive functions of Lactobacillus phage øg1e: cloning, sequence analysis, and expression in Escherichia coli

Material type: 文書・図像類

Author: KAKIKAWA, Makikoほか

Publisher: Elsevier Science B.V.

Publication date: 1997-01

Material Format: Digital

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Note (General)：: øg1e is a temperate phage of the Lactobacillus strain G1e. The phage-host junctions attR and attL cloned from the lysogen have a 24-bp common (core) s...

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Material Type: 文書・図像類
Title: Characterization of the genes encoding integrative and excisive functions of Lactobacillus phage øg1e: cloning, sequence analysis, and expression in Escherichia coli
Author/Editor: KAKIKAWA, Makiko
OKI, Masaya
WATANABE, Nobuyuki
YASUKAWA, Hiroo
MASAMUNE, Yukito
TAKETO, Akira
KODAIRA, Ken-Ichi
Author Heading: KAKIKAWA, Makiko
OKI, Masaya
WATANABE, Nobuyuki
YASUKAWA, Hiroo
MASAMUNE, Yukito
TAKETO, Akira
KODAIRA, Ken-Ichi
Publication, Distribution, etc.: Elsevier Science B.V.
Publication Date: 1997-01
Publication Date (W3CDTF): 1997-01
Periodical title: Gene -Amsterdam-
No. or year of volume/issue: 185 1
Volume: 185
Issue: 1
Pages: 119-125
Text Language Code: eng
Subject Heading: Bacteriophage øg1e
Lactic acid bacteria
Integrase
Excisionase
DNA sequence
Target Audience: 一般
Note (General): øg1e is a temperate phage of the Lactobacillus strain G1e. The phage-host junctions attR and attL cloned from the lysogen have a 24-bp common (core) sequence implicated in recombination. DNA sequencing analysis of a 5.2-kbp SacI fragment of the øg1e phage genome (42.5 kbp) revealed two possible open reading frames (ORF), xis and int, and the phage attachment (recombination) site (attP), whose 24-bp sequence is identical to the core sequence detected in attR and attL. The deduced int product (Int) is a basic protein of 391 amino acids with an estimated pI of 9.70, and significantly resembles other presumed integrases encoded by the Lactobacillus and Lactococcus phages including øadh and øLC3, as well as the Escherichia coli phages such as λ.The predicted øg1e xis protein (Xis) is small and very acidic (66 amino acids; pI 4.55), and shows a resemblance (32% overall identity) with a putative excisionase encoded by the Staphylococcus phage ø11. The øg1e Int with a deduced molecular mass of 45.5 kDa was overproduced in E. coli cells, and electrophoretically analyzed.
Access Restrictions: 限定公開
Related Material (DOI): 10.1016/S0378-1119(96)00648-8
Data Provider (Database): 国立情報学研究所 : 学術機関リポジトリデータベース（IRDB）（機関リポジトリ）
https://irdb.nii.ac.jp
Original Data Provider (Database): 福井大学 : 福井大学学術機関リポジトリ