Homology of myosin light chains, troponin-C and parvalbumins deduced from comparison of their amino acid sequences

1974 ◽  
Vol 58 (1) ◽  
pp. 301-308 ◽  
Author(s):  
John H. Collins
1991 ◽  
Vol 12 (4) ◽  
pp. 321-332 ◽  
Author(s):  
Winifred W. Barouch ◽  
Kimberly E. Breese ◽  
Stephanie -Alexis Davidoff ◽  
John Leszyk ◽  
Andrew G. Szent-Györgyi ◽  
...  

1989 ◽  
Vol 264 (30) ◽  
pp. 18247-18259
Author(s):  
T Kobayashi ◽  
T Takagi ◽  
K Konishi ◽  
W Wnuk

2003 ◽  
Vol 14 (9) ◽  
pp. 3650-3663 ◽  
Author(s):  
Diane M. Casey ◽  
Kazuo Inaba ◽  
Gregory J. Pazour ◽  
Saeko Takada ◽  
Ken-ichi Wakabayashi ◽  
...  

The outer dynein arm-docking complex (ODA-DC) is a microtubule-associated structure that targets the outer dynein arm to its binding site on the flagellar axoneme ( Takada et al. 2002 . Mol. Biol. Cell 13, 1015–1029). The ODA-DC of Chlamydomonas contains three proteins, referred to as DC1, DC2, and DC3. We here report the isolation and sequencing of genomic and full-length cDNA clones encoding DC3. The sequence predicts a 21,341 Da protein with four EF-hands that is a member of the CTER (calmodulin, troponin C, essential and regulatory myosin light chains) group and is most closely related to a predicted protein from Plasmodium. The DC3 gene, termed ODA14, is intronless. Chlamydomonas mutants that lack DC3 exhibit slow, jerky swimming because of loss of some but not all outer dynein arms. Some outer doublet microtubules without arms had a “partial” docking complex, indicating that DC1 and DC2 can assemble in the absence of DC3. In contrast, DC3 cannot assemble in the absence of DC1 or DC2. Transformation of a DC3-deletion strain with the wild-type DC3 gene rescued both the motility phenotype and the structural defect, whereas a mutated DC3 gene was incompetent to rescue. The results indicate that DC3 is important for both outer arm and ODA-DC assembly.


1971 ◽  
Vol 68 (10) ◽  
pp. 2569-2573 ◽  
Author(s):  
E. Appella ◽  
A. Chersi ◽  
O. A. Roholt ◽  
D. Pressman

1992 ◽  
Vol 204 (1) ◽  
pp. 85-91 ◽  
Author(s):  
Ana Claudia Rasera SILVA ◽  
John KENDRICK-JONES ◽  
Fernando C. REINACH

1970 ◽  
Vol 117 (4) ◽  
pp. 641-660 ◽  
Author(s):  
E. M. Press ◽  
N. M. Hogg

The amino acid sequences of the Fd fragments of two human pathological immunoglobulins of the immunoglobulin G1 class are reported. Comparison of the two sequences shows that the heavy-chain variable regions are similar in length to those of the light chains. The existence of heavy chain variable region subgroups is also deduced, from a comparison of these two sequences with those of another γ 1 chain, Eu, a μ chain, Ou, and the partial sequence of a fourth γ 1 chain, Ste. Carbohydrate has been found to be linked to an aspartic acid residue in the variable region of one of the γ 1 chains, Cor.


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