PMID- 16367966
OWN - NLM
STAT- MEDLINE
DCOM- 20060321
LR  - 20240109
IS  - 0960-7412 (Print)
IS  - 0960-7412 (Linking)
VI  - 45
IP  - 2
DP  - 2006 Jan
TI  - The Arabidopsis heavy metal P-type ATPase HMA5 interacts with metallochaperones 
      and functions in copper detoxification of roots.
PG  - 225-36
AB  - Since copper (Cu) is essential in key physiological oxidation reactions, 
      organisms have developed strategies for handling Cu while avoiding its 
      potentially toxic effects. Among the tools that have evolved to cope with Cu is a 
      network of Cu homeostasis factors such as Cu-transporting P-type ATPases that 
      play a key role in transmembrane Cu transport. In this work we present the 
      functional characterization of an Arabidopsis Cu-transporting P-type ATPase, 
      denoted heavy metal ATPase 5 (HMA5), and its interaction with Arabidopsis 
      metallochaperones. HMA5 is primarily expressed in roots, and is strongly and 
      specifically induced by Cu in whole plants. We have identified and characterized 
      plants carrying two independent T-DNA insertion alleles, hma5-1 and hma5-2. Both 
      mutants are hypersensitive to Cu but not to other metals such as iron, zinc or 
      cadmium. Interestingly, root tips from Cu-treated hma5 mutants exhibit a 
      wave-like phenotype at early stages and later on main root growth completely 
      arrests whereas lateral roots emerge near the crown. Accordingly, these lines 
      accumulate Cu in roots to a greater extent than wild-type plants under Cu excess. 
      Finally, yeast two-hybrid experiments demonstrate that the metal-binding domains 
      of HMA5 interact with Arabidopsis ATX1-like Cu chaperones, and suggest a 
      regulatory role for the plant-specific domain of the CCH Cu chaperone. Based on 
      these findings, we propose a role for HMA5 in Cu compartmentalization and 
      detoxification.
FAU - Andres-Colas, Nuria
AU  - Andres-Colas N
AD  - Departament de Bioquimica i Biologia Molecular, Universitat de Valencia, Av. Dr 
      Moliner, 50, E-46100 Burjassot, Valencia, Spain.
FAU - Sancenon, Vicente
AU  - Sancenon V
FAU - Rodriguez-Navarro, Susana
AU  - Rodriguez-Navarro S
FAU - Mayo, Sonia
AU  - Mayo S
FAU - Thiele, Dennis J
AU  - Thiele DJ
FAU - Ecker, Joseph R
AU  - Ecker JR
FAU - Puig, Sergi
AU  - Puig S
FAU - Penarrubia, Lola
AU  - Penarrubia L
LA  - eng
GR  - GM41840/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Plant J
JT  - The Plant journal : for cell and molecular biology
JID - 9207397
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (DNA Primers)
RN  - 0 (Molecular Chaperones)
RN  - 0 (RNA, Messenger)
RN  - 789U1901C5 (Copper)
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
SB  - IM
MH  - Adenosine Triphosphatases/chemistry/genetics/*metabolism
MH  - Amino Acid Sequence
MH  - Arabidopsis/*enzymology
MH  - Arabidopsis Proteins/chemistry/genetics/*metabolism
MH  - Base Sequence
MH  - Copper/*metabolism
MH  - DNA Primers
MH  - Genes, Plant
MH  - Molecular Chaperones/*metabolism
MH  - Molecular Sequence Data
MH  - Plant Roots/*metabolism
MH  - RNA, Messenger/genetics
MH  - Sequence Homology, Amino Acid
EDAT- 2005/12/22 09:00
MHDA- 2006/03/22 09:00
CRDT- 2005/12/22 09:00
PHST- 2005/12/22 09:00 [pubmed]
PHST- 2006/03/22 09:00 [medline]
PHST- 2005/12/22 09:00 [entrez]
AID - TPJ2601 [pii]
AID - 10.1111/j.1365-313X.2005.02601.x [doi]
PST - ppublish
SO  - Plant J. 2006 Jan;45(2):225-36. doi: 10.1111/j.1365-313X.2005.02601.x.