PMID- 24369789
OWN - NLM
STAT- MEDLINE
DCOM- 20140812
LR  - 20211021
IS  - 1471-2229 (Electronic)
IS  - 1471-2229 (Linking)
VI  - 13
DP  - 2013 Dec 27
TI  - The sequence flanking the N-terminus of the CLV3 peptide is critical for its 
      cleavage and activity in stem cell regulation in Arabidopsis.
PG  - 225
LID - 10.1186/1471-2229-13-225 [doi]
AB  - BACKGROUND: Although it is known that CLAVATA3 (CLV3) acts as 12- and/or 13-amino 
      acid (AA) secreted peptides to regulate the number of stem cells in shoot apical 
      meristems (SAMs), how functional CLV3 peptides are generated and if any 
      particular sequences are required for the processing remain largely unknown. 
      RESULTS: We developed a mass spectrometry (MS)-based in vitro assay to monitor 
      the cleavage of heterologously produced CLV3 fusion protein. Through 
      co-cultivation of the fusion protein with Arabidopsis seedlings, we identified 
      two cleavage sites: the previously reported one before Arg70 and a new one before 
      Met39. Using synthetic peptides together with MALDI-Tof-MS analyses, we 
      demonstrated that the non-conserved 5-AA motifs flanking N-termini of the CLV3 
      and its orthologous CLE1 peptides were critical for their cleavages and optimal 
      activities in vitro. We also found that substitutions of Leu69 by Ala in fusion 
      protein and in synthetic peptide of CLV3 compromised their cleavages, leading to 
      significantly reduced activities in regulating the sizes of shoot and root 
      meristems. CONCLUSIONS: These results suggest that 5-AA residues flanking the 
      N-terminus of CLV3 peptide are required for proper cleavages and optimal function 
      in stem cell regulation.
FAU - Xu, Ting-Ting
AU  - Xu TT
FAU - Song, Xiu-Fen
AU  - Song XF
FAU - Ren, Shi-Chao
AU  - Ren SC
FAU - Liu, Chun-Ming
AU  - Liu CM
AD  - Key Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese 
      Academy of Sciences, Nanxincun 20, Fragrant Hill, Beijing 100093, China. 
      cmliu@ibcas.ac.cn.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20131227
PL  - England
TA  - BMC Plant Biol
JT  - BMC plant biology
JID - 100967807
RN  - 0 (AT2G27250 protein, Arabidopsis)
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (Peptides)
RN  - 0 (Recombinant Fusion Proteins)
RN  - GMW67QNF9C (Leucine)
SB  - IM
MH  - Amino Acid Motifs
MH  - Amino Acid Sequence
MH  - Arabidopsis/*cytology/*metabolism
MH  - Arabidopsis Proteins/*chemistry/*metabolism
MH  - Biological Assay
MH  - Leucine/metabolism
MH  - Molecular Sequence Data
MH  - Peptides/chemistry
MH  - Plant Roots/metabolism
MH  - Recombinant Fusion Proteins/isolation & purification
MH  - Seedlings/growth & development
MH  - Sequence Alignment
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH  - Stem Cells/*cytology/metabolism
MH  - Structure-Activity Relationship
PMC - PMC3878228
EDAT- 2013/12/29 06:00
MHDA- 2014/08/13 06:00
PMCR- 2013/12/27
CRDT- 2013/12/28 06:00
PHST- 2013/09/21 00:00 [received]
PHST- 2013/12/20 00:00 [accepted]
PHST- 2013/12/28 06:00 [entrez]
PHST- 2013/12/29 06:00 [pubmed]
PHST- 2014/08/13 06:00 [medline]
PHST- 2013/12/27 00:00 [pmc-release]
AID - 1471-2229-13-225 [pii]
AID - 10.1186/1471-2229-13-225 [doi]
PST - epublish
SO  - BMC Plant Biol. 2013 Dec 27;13:225. doi: 10.1186/1471-2229-13-225.