A 46 kDa integral membrane protein from Mycobacterium leprae resembles a number of bacterial and mammalian membrane transport proteins
| Autor: | Guus H. Jarings, Linda Oskam, Paul R. Klatser, Madeleine Y.L. de Wit, Caroline J. Hermans, Robert D. Nicholls, Rudy A. Hartskeerl |
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| Přispěvatelé: | Other departments |
| Jazyk: | angličtina |
| Rok vydání: | 1995 |
| Předmět: |
Vesicle-associated membrane protein 8
Recombinant Fusion Proteins Blotting Western Molecular Sequence Data Microbiology HSPA4 Bacterial Proteins SNAP23 HSPA2 Amino Acid Sequence Cloning Molecular Integral membrane protein Hypopigmentation Antigens Bacterial HSPA14 biology Base Sequence Membrane transport protein Chromosome Mapping Membrane Proteins Biological Transport Peptide Fragments Mycobacterium leprae Biochemistry Membrane protein Genes Bacterial biology.protein |
| Zdroj: | Microbiology (Reading, England), 141 ( Pt 8), 1963-1968. Society for General Microbiology |
| ISSN: | 1350-0872 |
| DOI: | 10.1099/13500872-141-8-1963 |
| Popis: | In this paper we describe the nucleotide sequence of a 3·4 kbp region of the Mycobacterium leprae genome. This region contains an open reading frame of 1290 bp with a coding capacity for a protein of 46179 Da, designated the 38L protein. Using antibodies against part of the 38L protein, we were able to demonstrate that the 38L protein is present in the membrane protein fraction of M. leprae. The 38L protein showed significant matches with a number of integral membrane proteins involved in the transport of small molecules through the cellular membrane. Among these are a human and a murine protein involved in melanin biosynthesis. The 38L protein might play a role in the hypopigmentation observed in leprosy patients. |
| Databáze: | OpenAIRE |
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