NH2-terminal sequence of macrophage-expressed natural resistance- associated macrophage protein (Nramp) encodes a proline/serine-rich putative Src homology 3-binding domain

NH2-terminal sequence of macrophage-expressed natural resistance- associated macrophage protein (Nramp) encodes a proline/serine-rich putative Src homology 3-binding domain

The Lsh/Ity/Bcg locus on mouse chromosome 1 regulates macrophage (m phi) priming/activation for antimicrobial activity against intracellular pathogens. A candidate Bcg gene, designated natural resistance-associated m phi protein (Nramp), recently isolated from a pre-B cell cDNA library encodes a pol...

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Format: Online
Language:English
Published: The Rockefeller University Press 1994
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2191468/
id pubmed-2191468
recordtype oai_dc
spelling pubmed-21914682008-04-16 NH2-terminal sequence of macrophage-expressed natural resistance- associated macrophage protein (Nramp) encodes a proline/serine-rich putative Src homology 3-binding domain Articles The Lsh/Ity/Bcg locus on mouse chromosome 1 regulates macrophage (m phi) priming/activation for antimicrobial activity against intracellular pathogens. A candidate Bcg gene, designated natural resistance-associated m phi protein (Nramp), recently isolated from a pre-B cell cDNA library encodes a polytopic integral membrane protein with structural features common to prokaryotic and eukaryotic transporters. In the present study, an activated m phi cDNA library yielded new Nramp clones that differ in the 5' region from the published pre-B cell-derived clone sequence, resulting in addition of 64 amino acids at the NH2 terminus of the predicted protein. This new domain is rich in proline, serine, and basic amino acids, and includes three protein kinase C phosphorylation sites and a putative Src homology 3 binding domain. RNAs containing this domain are the only form found in the m phi. Hence, the protein encoded by this RNA is the candidate molecule mediating natural resistance to intra-m phi pathogens. The Rockefeller University Press 1994-05-01 /pmc/articles/PMC2191468/ /pubmed/7513015 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
title NH2-terminal sequence of macrophage-expressed natural resistance- associated macrophage protein (Nramp) encodes a proline/serine-rich putative Src homology 3-binding domain
spellingShingle NH2-terminal sequence of macrophage-expressed natural resistance- associated macrophage protein (Nramp) encodes a proline/serine-rich putative Src homology 3-binding domain
title_short NH2-terminal sequence of macrophage-expressed natural resistance- associated macrophage protein (Nramp) encodes a proline/serine-rich putative Src homology 3-binding domain
title_full NH2-terminal sequence of macrophage-expressed natural resistance- associated macrophage protein (Nramp) encodes a proline/serine-rich putative Src homology 3-binding domain
title_fullStr NH2-terminal sequence of macrophage-expressed natural resistance- associated macrophage protein (Nramp) encodes a proline/serine-rich putative Src homology 3-binding domain
title_full_unstemmed NH2-terminal sequence of macrophage-expressed natural resistance- associated macrophage protein (Nramp) encodes a proline/serine-rich putative Src homology 3-binding domain
title_sort nh2-terminal sequence of macrophage-expressed natural resistance- associated macrophage protein (nramp) encodes a proline/serine-rich putative src homology 3-binding domain
description The Lsh/Ity/Bcg locus on mouse chromosome 1 regulates macrophage (m phi) priming/activation for antimicrobial activity against intracellular pathogens. A candidate Bcg gene, designated natural resistance-associated m phi protein (Nramp), recently isolated from a pre-B cell cDNA library encodes a polytopic integral membrane protein with structural features common to prokaryotic and eukaryotic transporters. In the present study, an activated m phi cDNA library yielded new Nramp clones that differ in the 5' region from the published pre-B cell-derived clone sequence, resulting in addition of 64 amino acids at the NH2 terminus of the predicted protein. This new domain is rich in proline, serine, and basic amino acids, and includes three protein kinase C phosphorylation sites and a putative Src homology 3 binding domain. RNAs containing this domain are the only form found in the m phi. Hence, the protein encoded by this RNA is the candidate molecule mediating natural resistance to intra-m phi pathogens.
publisher The Rockefeller University Press
publishDate 1994
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2191468/
_version_ 1611429886517313536

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