Overexpression, Purification, and Analysis of Complementation Behavior of E. coli SuhB Protein: Comparison with Bacterial and Archaeal Inositol Monophosphatases-Reference-Cited by-同舟云学术

Overexpression, Purification, and Analysis of Complementation Behavior of E. coli SuhB Protein: Comparison with Bacterial and Archaeal Inositol Monophosphatases

Published:2000-03-11 Issue:14 Volume:39 Page:4145-4153
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Chen Liangjing¹,Roberts Mary F.¹

Affiliation:

1. Merkert Chemistry Center, Boston College, Chestnut Hill, Massachusetts 02467

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi992424f

Reference35 articles.

1. Mutation that suppresses the protein export defect of the secY mutation and causes cold-sensitive growth of Escherichia coli

2. A defined mutation in the protein export gene within the spc ribosomal protein operon of Escherichia coli: isolation and characterization of a new temperature-sensitive secY mutant.

3. A mutation that enhances synthesis of sigma 32 and suppresses temperature-sensitive growth of the rpoH15 mutant of Escherichia coli

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2. SuhB is an integral part of the ribosomal antitermination complex and interacts with NusA;Nucleic Acids Research;2019-05-25

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