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Article

Interaction of the Escherichia coli lipoprotein NlpI with periplasmic Prc (Tsp) protease.

Journal of biochemistry - 1 Feb 2004

Tadokoro Akiko, Hayashi Hidemi, Kishimoto Toshihiko, Makino Yasutaka, Fujisaki Shingo, Nishimura Yukinobu

Abstract excerpt

Escherichia coli spr (suppressor of prc) mutants and nlpI mutants show thermosensitive growth. The thermosensitivity of the spr mutants was suppressed by the nlpI mutations. Expression of the fusion genes encoding hexa-histidine-tagged NlpI (NlpI-His) and purification of the tagged NlpI showed that NlpI-His bound with Prc protease and IbpB chaperone. NlpI-His with the amino acid substitution of G103D did not bind...

Topics

Amino Acid Sequence
Base Sequence
Endopeptidases
Escherichia coli
Escherichia coli Proteins
Hot Temperature
Lipoproteins
Molecular Sequence Data
Mutation
Plasmids
Time Factors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 15047720
DOI: 10.1093/jb/mvh022

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