Molecular dissection of the Erv41-Erv46 retrograde receptor reveals a conserved cysteine-rich region in Erv46 required for retrieval activity

The retrograde cargo receptor Erv41-Erv46 retrieves non–KDEL-bearing ER resident proteins to maintain ER homeostasis. This study defines a conserved cysteine-rich element in Erv46 that is required for retrieval activity and cargo binding. We propose that disulfides within the cysteine-rich region regulate the hydrophobic cargo binding site.

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Map-based cloning of a gene sequence encoding a nucleotide-binding domain and a leucine-rich region at the Cre3 nematode resistance locus of wheat

Genome ◽

10.1139/g97-087 ◽

1997 ◽

Vol 40 (5) ◽

pp. 659-665 ◽

Cited By ~ 87

Author(s):

Evans S. Lagudah ◽

Odile Moullet ◽

Rudi Appels

Keyword(s):

Disease Resistance ◽

Gene Family ◽

Binding Site ◽

Resistance Gene ◽

Resistance Genes ◽

Gene Sequence ◽

Nucleotide Binding ◽

Disease Resistance Gene ◽

Leucine Rich Repeat ◽

Rich Region

The Cre3 gene confers a high level of resistance to the root endoparasitic nematode Heterodera avenae in wheat. A DNA marker cosegregating with H. avenae resistance was used as an entry point for map-based cloning of a disease resistance gene family at the Cre3 locus. Two related gene sequences have been analysed at the Cre3 locus. One, identified as a cDNA clone, encodes a polypeptide with a nucleotide binding site (NBS) and a leucine-rich region; this member of the disease resistance gene family is expressed in roots. A second Cre3 gene sequence, cloned as genomic DNA, appears to be a pseudogene, with a frame shift caused by a deletion event. These two genes, related to members of the cytoplasmic NBS – leucine rich repeat class of plant disease resistance genes were physically mapped to the distal 0.06 fragment of the long arm of wheat chromosome 2D and cosegregated with nematode resistance.Key words: cereal cyst nematode, disease resistance genes, nucleotide-binding site, leucine-rich repeat.

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Three noncontiguous peptides comprise binding sites on high-molecular-weight kininogen to neutrophils

AJP Heart and Circulatory Physiology ◽

10.1152/ajpheart.1998.275.1.h145 ◽

1998 ◽

Vol 275 (1) ◽

pp. H145-H150 ◽

Cited By ~ 1

Author(s):

Mohammad M. H. Khan ◽

Satya P. Kunapuli ◽

Yingzhang Lin ◽

Abraham Majluf-Cruz ◽

Raul A. Dela Cadena ◽

...

Keyword(s):

Molecular Weight ◽

Binding Site ◽

High Molecular Weight ◽

Binding Sites ◽

Polymorphonuclear Leukocytes ◽

High Molecular Weight Kininogen ◽

Rich Region ◽

Putative Receptor ◽

Exon 9 ◽

Stimulation Of

The binding of high-molecular-weight kininogen (HK) to neutrophils (polymorphonuclear leukocytes, PMN) is required for the stimulation of aggregation and degranulation by human plasma kallikrein as well as the displacement of fibrinogen from this cell surface. The putative receptor for HK is the leukocyte integrin αMβ2, and domains 3 (D3) and 5 (D5) of HK form its binding site. To further map the binding sites on HK for PMN, we used D3 recombinant exon products and designed peptides from D3 and D5. In D3, a heptapeptide, Leu271-Ala277, from exon 7 product, and a peptide, Cys333-Cys352, from exon 9 product can inhibit binding of kininogen to PMN. Two contiguous peptides from D5 in the histidine-glycine-rich region, Gly442-Lys458and Phe459-Lys478, each inhibit the binding of HK to PMN. This study has thus delineated three noncontiguous surface-oriented sequences on HK, which together comprise all or most of the binding site for human PMN.

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