Download Supplemental Figures and Tables

Supplemental Figure 1. The REVOLUTA M-WD40 subdomain shows similarities to
the WD40 domain.
Multiple sequence alignment of the Arabidopsis REV M-WD40 subdomain, the
Thermomonospora curvata PKWA WD40 domain and the WD40 domain 50% consensus
sequence as annotated by the Simple Modular Architecture Research Tool (Schultz et al.,
1998). Amino acid grouping: s (A,C,D,G,N,P,S,T,V), p (C,D,E,H,K,N,Q,R,S,T), l
(I,L,V), u (A,G,S), a (F,H,W,Y), o (S,T), h (A,C,F,G,H,I,K,L,M,R,T,V,W,Y), + (H,K,R).
Schultz, J., Milpetz, F., Bork, P., Ponting, C.P. (1998). SMART, a simple
modular architecture research tool: identification of signaling domains. Proc Natl Acad
Sci USA 95: 5857-64.
Supplemental Figure 2. The leucine zipper domain is necessary for REVOLUTA
transcriptional activation activity in vivo.
(A) Homo-dimerization yeast two hybrid assays. The same proteins were used as bait
(fused to GAL4 DNA binding domain) and prey (fused to GAL4 activation domain).
(B) GUS expression in leaf abaxial (lower) epidermal cells of tobacco transiently
transformed with pZPR3-uidA and 35S-REV* or pZPR3-uidA and 35S-REV*-ΔLZ
constructs. microRNA resistant REV is designated REV*. REV homo-dimerization
through the leucine zipper domain is schematically represented by two strings of leucines
(L) touching each other.
(C) YFP-fusion assays in tobacco leaf abaxial (lower) epidermal cells transiently
transformed. Scale bar, 100 μm.
Supplemental Figure 3. Multiple sequence alignment of the Arabidopsis thaliana, Oryza
sativa, Ginkgo biloba, Pinus taeda, Psilotum nudum, Physcomitrella patens, and
Chlamydomonas reinhardtii MEKHLA domains used to generate the Neighbor-Joining
tree in Figure 1C.
Supplemental Figure 4. Multiple sequence alignment of the Arabidopsis thaliana, Oryza
sativa, Ginkgo biloba, Pinus taeda, Psilotum nudum, and Physcomitrella patens HD-ZIP
III proteins used to generate the Neighbor-Joining and Maximum-Parsimony trees built to
corroborate the tree in Figure 1C.
Supplemental Figure 5. Yeast two hybrid assays. Positive interactions were detected by
assaying for β-galactosidase activity at eight and 24 hours. Top row are standards for
interaction. -, pDEST32/pDEST22. +, pPC97-RB/pPC86-E2F1. ++, pPC97-CYH2–
dDP/pPC86-dE2F. +++, pPC97-Fos/pPC86-Jun. 1, pDEST32-REV/pDEST22-REV. 2,
pDEST32-REV-ΔMEKHLA/pDEST22-REV-ΔMEKHLA.
3,
pDEST32-REV-
ΔS2/pDEST22-REV-ΔS2. 4, pDEST32-REV-ΔS1S2-16aa/pDEST22-REV-ΔS1S2-16aa. 5,
pDEST32-REV/pDEST22-PHB.
6,
pDEST32-REV-ΔMEKHLA/pDEST22-PHB.
pDEST32-REV/pDEST22-PHB-ΔMEKHLA.
PHB-ΔMEKHLA.
8,
7,
pDEST32-REV-ΔMEKHLA/pDEST22-
Sequence name
REV
REV-S2
REV-PAS
REV-MEKHLA
REV-HD-LZ
REV-HD
REV-START-HDSAD
REV-START
REV-HDSAD
REV-MEKHLA
REV-PAS
REV-MEKHLA-S2
REV-M-WD40
REV-S1S2
REV-LEU
REV-AASE
PHB
PHB-MEKHLA
ATHB8
ATHB8-MEKHLA
ChlamyMEKHLA
GL2
ZPR3
* Relative to A in starting ATG
Supplemental Table 1. Sequences used in this study.
Sequence coordinates*
1-2529
1-2231
1-2187
1-2058
1-453
1-267
383-2058
383-1134
1111-2058
2059-2529
2188-2529
2059-2231
2059-2187
1-2229
1-266375-2529
1-25062511-2529
1-2559
1-2094
1-2502
1-2049
241-708
1-2244
1-204