PMID- 10412910
OWN - NLM
STAT- MEDLINE
DCOM- 19990803
LR  - 20190822
IS  - 0167-4412 (Print)
IS  - 0167-4412 (Linking)
VI  - 40
IP  - 2
DP  - 1999 May
TI  - A novel E-type endo-beta-1,4-glucanase with a putative cellulose-binding domain 
      is highly expressed in ripening strawberry fruits.
PG  - 323-32
AB  - Two full-length cDNA clones (faEG1 and faEG3, respectively) have been isolated by 
      screening a cDNA library representing transcripts from red strawberry fruits. 
      Southern blot analysis of genomic DNA suggests that the strawberry 
      endo-beta-1,4-glucanases (EGases) are encoded by a multigene family. The cognate 
      genes are predominantly expressed during the ripening process proper, although, 
      in the case of faEG3, some expression has also been observed in large green 
      fruits and, at low amounts, in young vegetative green tissues. In agreement with 
      other ripening-related genes in strawberry, also the expression of faEG1 and 
      faEG3 is down-regulated by treatment with an auxin analogue (1-naphthaleneacetic 
      acid, NAA). Differences in temporal expression of the two EGase genes in fruits 
      are not accompanied by differences in spatial expression. The pattern of 
      expression and the sequence characteristics of the two polypeptides suggest that 
      the two strawberry EGases operate in a synergistic and coordinate manner. The 
      protein encoded by faEG1 looks like one of the usual higher-plant EGases (average 
      molecular mass of 54 kDa), while the protein encoded by faEG3 has a greater 
      deduced molecular mass (about 68 kDa) due to the presence of an extra peptide of 
      about 130 amino acids at the C-terminus. Such unusual peptide shows some features 
      also found in microbial cellulases and contains a putative cellulose-binding 
      domain. We propose that the faEG3-encoded EGase might especially hydrolyse the 
      xyloglucans coating the cellulose microfibrils, thus rendering the cell wall more 
      susceptible to the subsequent hydrolytic activity of the faEG1-encoded EGase.
FAU - Trainotti, L
AU  - Trainotti L
AD  - Dipartimento di Biologia, Universita di Padova, Italy.
FAU - Spolaore, S
AU  - Spolaore S
FAU - Pavanello, A
AU  - Pavanello A
FAU - Baldan, B
AU  - Baldan B
FAU - Casadoro, G
AU  - Casadoro G
LA  - eng
SI  - GENBANK/AJ006348
SI  - GENBANK/AJ006349
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Plant Mol Biol
JT  - Plant molecular biology
JID - 9106343
RN  - 0 (DNA, Complementary)
RN  - 0 (Indoleacetic Acids)
RN  - 0 (Isoenzymes)
RN  - 63231-63-0 (RNA)
RN  - 9004-34-6 (Cellulose)
RN  - EC 3.2.1.4 (Cellulase)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Cellulase/*genetics/metabolism
MH  - Cellulose/*metabolism
MH  - DNA, Complementary/chemistry/genetics
MH  - Fruit/enzymology/*genetics/growth & development
MH  - Gene Expression/drug effects
MH  - Gene Expression Regulation, Developmental
MH  - Gene Expression Regulation, Enzymologic
MH  - Gene Expression Regulation, Plant
MH  - In Situ Hybridization
MH  - Indoleacetic Acids/pharmacology
MH  - Isoenzymes/genetics
MH  - Molecular Sequence Data
MH  - RNA/drug effects/genetics/metabolism
MH  - Sequence Alignment
MH  - Sequence Analysis, DNA
MH  - Sequence Homology, Amino Acid
EDAT- 1999/07/21 00:00
MHDA- 1999/07/21 00:01
CRDT- 1999/07/21 00:00
PHST- 1999/07/21 00:00 [pubmed]
PHST- 1999/07/21 00:01 [medline]
PHST- 1999/07/21 00:00 [entrez]
AID - 10.1023/a:1006299821980 [doi]
PST - ppublish
SO  - Plant Mol Biol. 1999 May;40(2):323-32. doi: 10.1023/a:1006299821980.