A myosin-like protein from a higher plant.
As part of a study of the diversity of myosins, we have cloned a cDNA encoding a myosin-like protein from Arabidopsis thaliana. This is the first molecular motor of any kind to be cloned from a higher plant. The predicted polypeptide (molecular weight 131 kDa) has a motor domain (head) very similar to those of other myosins, but the remainder of the sequence is unusual. The tail contains four potential calmodulin binding sites ("IQ-motifs"), but no sequence motifs suggestive of actin or phospholipid binding, like those found in other myosins. There is also a small region of probable alpha-helical coiled-coil, which suggests that the molecule could be dimeric, though unlikely to form filaments. The N-terminal and C-terminal regions of the molecule are unique. We present a phylogenetic analysis of myosin head sequences, which suggests that this is a new type of myosin.
Knight
A E
AE
MRC Laboratory of Molecular Biology, Cambridge, U.K.
Kendrick-Jones
J
J
D000595:Amino Acid Sequence; D000818:Animals; D017360:Arabidopsis / Q000235:genetics*; D001483:Base Sequence; D015152:Blotting, Northern; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D015723:Gene Library; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009218:Myosins / Q000235:genetics* / Q000302:isolation & purification; D009838:Oligodeoxyribonucleotides; D010802:Phylogeny; D010940:Plant Proteins / Q000235:genetics* / Q000302:isolation & purification; D011061:Poly A / Q000235:genetics / Q000302:isolation & purification; D016133:Polymerase Chain Reaction; D012313:RNA / Q000235:genetics / Q000302:isolation & purification; D012333:RNA, Messenger; D015183:Restriction Mapping; D017386:Sequence Homology, Amino Acid
D009838:Oligodeoxyribonucleotides; D010940:Plant Proteins; D012333:RNA, Messenger; D011061:Poly A; D012313:RNA; D004247:DNA; D009218:Myosins