PMID- 18624645
OWN - NLM
STAT- MEDLINE
DCOM- 20081006
LR  - 20080715
IS  - 0894-0282 (Print)
IS  - 0894-0282 (Linking)
VI  - 21
IP  - 6
DP  - 2008 Jun
TI  - Structure of the glucanase inhibitor protein (GIP) family from phytophthora 
      species suggests coevolution with plant endo-beta-1,3-glucanases.
PG  - 820-30
LID - 10.1094/MPMI-21-6-0820 [doi]
AB  - During invasion of their plant hosts, species of the oomycete genus Phytophthora 
      secrete glucanase inhibitor proteins (GIPs) into the plant apoplast, which bind 
      and inhibit the activity of plant extracellular endo-beta-1,3-glucanases 
      (EGases). GIPs show structural homology to the chymotrypsin class of serine 
      proteases (SP) but lack proteolytic activity due to the absence of an intact 
      catalytic triad and, thus, belong to a broader class of proteins called serine 
      protease homologs (SPH). To study the evolutionary relationship between GIPs and 
      functional SP, database searches were used to identify 48 GIP homologs in the P. 
      sojae, P. ramorum, and P. infestans genomes, composing GIPs, SPH, and potentially 
      functional SP. Analyses of P. infestans-inoculated tomato leaves showed that P. 
      infestans GIPs and tomato EGases are present in the apoplast and form stable 
      complexes in planta. Studies of the temporal expression of a four-membered GIP 
      family from P. infestans (PiGIP1 to PiGIP4) further revealed that the genes show 
      distinctly different patterns during an infection timecourse. Codon evolution 
      analyses of GIP homologs identified several positively selected peptide sites and 
      structural modeling revealed them to be in close proximity to rapidly evolving 
      EGase residues, suggesting that the interaction between GIPs and EGases has the 
      hallmarks of a coevolving molecular arms race.
FAU - Damasceno, Cynthia M B
AU  - Damasceno CM
AD  - Department of Plant Biology, Cornell University, Ithaca, NY 14853, U.S.A.
FAU - Bishop, John G
AU  - Bishop JG
FAU - Ripoll, Daniel R
AU  - Ripoll DR
FAU - Win, Joe
AU  - Win J
FAU - Kamoun, Sophien
AU  - Kamoun S
FAU - Rose, Jocelyn K C
AU  - Rose JK
LA  - eng
SI  - GENBANK/EU443391
SI  - GENBANK/EU443392
SI  - GENBANK/EU443393
SI  - GENBANK/EU443394
SI  - GENBANK/EU443395
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - Mol Plant Microbe Interact
JT  - Molecular plant-microbe interactions : MPMI
JID - 9107902
RN  - 0 (Algal Proteins)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (Plant Proteins)
RN  - EC 3.2.1.58 (Glucan 1,3-beta-Glucosidase)
SB  - IM
MH  - Algal Proteins/chemistry/*genetics/metabolism
MH  - Amino Acid Sequence
MH  - Blotting, Western
MH  - Enzyme Inhibitors/chemistry/*metabolism
MH  - *Evolution, Molecular
MH  - Glucan 1,3-beta-Glucosidase/chemistry/classification/*genetics
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Phylogeny
MH  - Phytophthora/genetics/*metabolism
MH  - Plant Proteins/chemistry/*genetics
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary
MH  - Reverse Transcriptase Polymerase Chain Reaction
MH  - Sequence Homology, Amino Acid
EDAT- 2008/07/16 09:00
MHDA- 2008/10/07 09:00
CRDT- 2008/07/16 09:00
PHST- 2008/07/16 09:00 [pubmed]
PHST- 2008/10/07 09:00 [medline]
PHST- 2008/07/16 09:00 [entrez]
AID - 10.1094/MPMI-21-6-0820 [doi]
PST - ppublish
SO  - Mol Plant Microbe Interact. 2008 Jun;21(6):820-30. doi: 10.1094/MPMI-21-6-0820.