Arabidopsis COPT1 copper transporter uses a single histidine to regulate transport activity and protein stability (Record no. 55240)

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fixed length control field 02358nam a2200289Ia 4500
003 - CONTROL NUMBER IDENTIFIER
control field MX-MdCICY
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20250625162502.0
040 ## - CATALOGING SOURCE
Transcribing agency CICY
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-21163
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 250602s9999 xx |||||s2 |||| ||und|d
245 10 - TITLE STATEMENT
Title Arabidopsis COPT1 copper transporter uses a single histidine to regulate transport activity and protein stability
490 0# - SERIES STATEMENT
Volume/sequential designation International Journal of Biological Macromolecules, 241, p.124404, 2023
520 3# - SUMMARY, ETC.
Summary, etc. Copper acquisition and subsequent delivery to target proteins are essential for many biological processes. However, the cellular levels of this trace element must be controlled because of its potential toxicity. The COPT1 protein rich in potential metal-binding amino acids functions in high affinity copper uptake at the plasma membrane of Arabidopsis cells. The functional role of these putative metal-binding residues is largely unknown. Through truncations and site-directed mutagenesis, we identified His43, a single residue within the extracellular N-terminal domain as absolutely critical for copper uptake of COPT1. Substitution of this residue with leucine, methionine or cysteine almost inactivated transport function of COPT1, implying that His43 fails to serves as a copper ligand in the regulation of COPT1 activity. Deletion of all extracellular N-terminal metal-binding residues completely blocked copper-stimulated degradation but did not alter the subcellular distribution and multimerization of COPT1. Although mutation of His43 to alanine and serine retained the transporter activity in yeast cells, the mutant protein was unstable and degraded in the proteasome in Arabidopsis cells. Our results demonstrate a pivotal role for the extracellular residue His43 in high affinity copper transport activity, and suggest common molecular mechanisms for regulating both metal transport and protein stability of COPT1.
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element COPPER TRANSPORTER
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element HISTIDINE
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element ARABIDOPSIS
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PROTEIN STABILITY
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element METAL LIGAND
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name He, L.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Ma, H.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Song, W.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Zhou, Z.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Ma, C.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Zhang, H.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/open?id=16FMrcK5rj6A32EHsKAnpf02gesw9f2We&usp=drive_copy">https://drive.google.com/open?id=16FMrcK5rj6A32EHsKAnpf02gesw9f2We&usp=drive_copy</a>
Public note Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Source of classification or shelving scheme Clasificación local
Koha item type Documentos solicitados
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Lost status Source of classification or shelving scheme Damaged status Not for loan Collection Home library Current library Shelving location Date acquired Total checkouts Full call number Date last seen Price effective from Koha item type
  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-21163 25.06.2025 25.06.2025 Documentos solicitados