Nucleotide sequence of the btuCED genes involved in vitamin B12 transport in Escherichia coli and homology with components of periplasmic-binding-protein-dependent transport systems
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| Published in: | Journal of Bacteriology Vol. 167; no. 3; pp. 928 - 934 |
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| AbstractList | The products of the btuCED region of the Escherichia coli chromosome participate in the transport of vitamin B12 across the cytoplasmic membrane. The nucleotide sequence of the 3,410-base-pair HindIII-HincII DNA fragment carrying a portion of the himA gene and the entire btuCED region was determined. Comparison of the location of the open reading frames with the gene boundaries defined by transposon insertions allowed the assignment of polypeptide products to gene sequences. The btuC product is a highly nonpolar integral membrane protein of molecular weight 31,683. The distribution of hydrophobic regions suggests the presence of numerous membrane-spanning domains. The btuD product is a relatively polar but membrane-associated polypeptide of Mr 27,088 and contains segments bearing extensive homology to the ATP-binding peripheral membrane constituents of periplasmic binding protein-dependent transport systems. Other regions of this protein are similar to portions of the outer membrane vitamin B12 receptor. The btuE product (Mr 20,474) appears to have a periplasmic location. It has the mean hydropathy of a soluble protein but lacks an obvious signal sequence. The cellular locations and structural and sequence homologies of the Btu polypeptides point to the similarity of these three proteins to components of binding protein-dependent transport systems. However, the dependence on a periplasmic vitamin B12-binding protein has not yet been demonstrated. Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology. For an alternate route to JB .asm.org, visit: JB |
| Author | L C de Veaux M J Friedrich R J Kadner |
| Author_xml | – sequence: 1 givenname: M. J surname: FRIEDRICH fullname: FRIEDRICH, M. J organization: Univ. Virginia, school medicine, Charlottesville VA 22908, United States – sequence: 2 givenname: L. C surname: DEVEAUX fullname: DEVEAUX, L. C organization: Univ. Virginia, school medicine, Charlottesville VA 22908, United States – sequence: 3 givenname: R. J surname: KADNER fullname: KADNER, R. J organization: Univ. Virginia, school medicine, Charlottesville VA 22908, United States |
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| Keywords | Nucleotide sequence Escherichia coli Homology Cyanocobalamin Binding protein Gene Aminoacid DNA Bacteria Chemical composition Transport Escherichieae Enterobacteriaceae |
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Mendeley... The products of the btuCED region of the Escherichia coli chromosome participate in the transport of vitamin B12 across the cytoplasmic membrane. The... |
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| StartPage | 928 |
| SubjectTerms | Amino Acid Sequence ATP-Binding Cassette Transporters Bacterial Proteins - genetics Bacteriology Base Sequence Biological and medical sciences Biological Transport Carrier Proteins - genetics Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Genes, Bacterial Genetics Membrane Proteins - genetics Microbiology Periplasmic Binding Proteins Sequence Homology, Nucleic Acid Vitamin B 12 - metabolism |
| Title | Nucleotide sequence of the btuCED genes involved in vitamin B12 transport in Escherichia coli and homology with components of periplasmic-binding-protein-dependent transport systems |
| URI | http://jb.asm.org/content/167/3/928.abstract https://www.ncbi.nlm.nih.gov/pubmed/3528129 https://search.proquest.com/docview/77005379 https://pubmed.ncbi.nlm.nih.gov/PMC215960 |
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