PMID- 1663947
OWN - NLM
STAT- MEDLINE
DCOM- 19920306
LR  - 20190510
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 110
IP  - 4
DP  - 1991 Oct
TI  - Characterization of calcium-binding light chain as a Ca(2+)-receptive subunit of 
      Physarum myosin.
PG  - 566-70
AB  - Physarum myosin is uniquely under an inhibitory Ca(2+)-regulation in the 
      ATP-dependent interaction with actin [Kohama (1990) Trends Pharmacol. Sci. 11, 
      433-435, for review]. Calcium-binding light chain (CaLc) has been suggested to be 
      of primary importance to the control from its amino acid sequence [Kobayashi et 
      al. (1988) J. Biol. Chem. 263, 305-313]. To provide a biochemical basis for this 
      suggestion, the Ca-binding capacity of CaLc and its Kd for Ca2+ were measured. 
      The Ca-binding properties of CaLc allowed those of Physarum myosin to be 
      explained in terms of CaLc. However, the mode of Ca(2+)-regulation by CaLc 
      differs according to the enzyme upon which Ca-sensitivity is confered by CaLc, 
      i.e., CaLc activated bovine phosphodiesterase activity and inhibited Physarum 
      myosin ATPase activity, with the same Kd in microM levels. Thus, CaLc appears to 
      work as a mere Ca-receptive subunit in Physarum myosin, with the secret of the 
      inhibition lying in other subunits. CaLc was also shown to belong to a family of 
      alkali light chains (AlLc) by allowing it to bind skeletal myosin as a substitute 
      for its AlLc. Therefore, present study is the first biochemical indication that 
      the AlLc family is involved in regulating the myosin function.
FAU - Kohama, K
AU  - Kohama K
AD  - Department of Pharmacology, Gunma University School of Medicine.
FAU - Okagaki, T
AU  - Okagaki T
FAU - Takano-Ohmuro, H
AU  - Takano-Ohmuro H
FAU - Ishikawa, R
AU  - Ishikawa R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Actins)
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Calmodulin)
RN  - 0 (Macromolecular Substances)
RN  - 214IZI85K3 (Trifluoperazine)
RN  - 9BZQ3U62JX (Dithionitrobenzoic Acid)
RN  - EC 3.1.4.- (Phosphoric Diester Hydrolases)
RN  - EC 3.6.4.1 (Myosins)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Actins/metabolism
MH  - Animals
MH  - Calcium/*metabolism/pharmacology
MH  - Calcium-Binding Proteins/isolation & purification/*metabolism
MH  - Calmodulin/metabolism
MH  - Dithionitrobenzoic Acid/pharmacology
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Kinetics
MH  - Macromolecular Substances
MH  - Molecular Weight
MH  - Myosins/*metabolism
MH  - Phosphoric Diester Hydrolases/metabolism
MH  - Physarum polycephalum/*metabolism
MH  - Trifluoperazine/pharmacology
EDAT- 1991/10/01 00:00
MHDA- 1991/10/01 00:01
CRDT- 1991/10/01 00:00
PHST- 1991/10/01 00:00 [pubmed]
PHST- 1991/10/01 00:01 [medline]
PHST- 1991/10/01 00:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a123620 [doi]
PST - ppublish
SO  - J Biochem. 1991 Oct;110(4):566-70. doi: 10.1093/oxfordjournals.jbchem.a123620.