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Axonemal radial spokes: 3D structure, function and assembly.

Pigino G, Ishikawa T - Bioarchitecture (2012)

Bottom Line: Despite numerous biochemical, physiological and structural studies, the mechanism of the function of the radial spoke remains unclear.Detailed knowledge of the 3D structure of the RS protein complex is needed in order to understand how RS regulates dynein activity.Here we review the most important findings on the structure of the RS, including results of our recent cryo-electron tomographic analysis of the RS protein complex.

View Article: PubMed Central - PubMed

ABSTRACT
The radial spoke (RS) is a complex of at least 23 proteins that works as a mechanochemical transducer between the central-pair apparatus and the peripheral microtubule doublets in eukaryotic flagella and motile cilia. The RS contributes to the regulation of the activity of dynein motors, and thus to flagellar motility. Despite numerous biochemical, physiological and structural studies, the mechanism of the function of the radial spoke remains unclear. Detailed knowledge of the 3D structure of the RS protein complex is needed in order to understand how RS regulates dynein activity. Here we review the most important findings on the structure of the RS, including results of our recent cryo-electron tomographic analysis of the RS protein complex.

No MeSH data available.


Related in: MedlinePlus

Figure 5. 3D structure of Chlamydomonas RS3 stump (RS3S). (A) RS3S in WT (left) and ida4 (right) flagella. The RS3S is colored in orange and IDA d/a in blue. The IDA d/a is missing in ida4 flagella. The arrows show the approximate position of the dynein d/a tail in WT and its corresponding location in ida4. In ida4, no densities are visible at this location as indicated by the blue dashed line. (View from the adjacent doublet microtubules. The proximal end of the axoneme is to the left.) (B) The structure of RS3S is unchanged in pf14 (purple), pf24 (turquoise), and pf1 (yellow) RS mutants. This indicates a different protein composition between RS3S and the other RSs. Bar, 25 nm.
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Figure 5: Figure 5. 3D structure of Chlamydomonas RS3 stump (RS3S). (A) RS3S in WT (left) and ida4 (right) flagella. The RS3S is colored in orange and IDA d/a in blue. The IDA d/a is missing in ida4 flagella. The arrows show the approximate position of the dynein d/a tail in WT and its corresponding location in ida4. In ida4, no densities are visible at this location as indicated by the blue dashed line. (View from the adjacent doublet microtubules. The proximal end of the axoneme is to the left.) (B) The structure of RS3S is unchanged in pf14 (purple), pf24 (turquoise), and pf1 (yellow) RS mutants. This indicates a different protein composition between RS3S and the other RSs. Bar, 25 nm.

Mentions: Maybe the most surprising discovery of our cryo‐tomographic analysis of Chlamydomonas RSs was a short structure located at precisely the same place where RS3 is located in Tetrahymena (Figs. 2A, 3Aand5). The positioning and the morphological similarity between this short structure in Chlamydomonas and the reconstructed base of RS3 in Tetrahymena indicate that the Chlamydomonas repeat contains, in addition to the doublet of RS1 and RS2, a portion of the RS3.2 This finding was further confirmed by a comparison of the structure of Chlamydomonas with the structure of RS3 in sea urchin sperm flagella.45 We introduced the name RS3 stump (RS3S) for the portion of RS3 that is present in Chlamydomonas.


Axonemal radial spokes: 3D structure, function and assembly.

Pigino G, Ishikawa T - Bioarchitecture (2012)

Figure 5. 3D structure of Chlamydomonas RS3 stump (RS3S). (A) RS3S in WT (left) and ida4 (right) flagella. The RS3S is colored in orange and IDA d/a in blue. The IDA d/a is missing in ida4 flagella. The arrows show the approximate position of the dynein d/a tail in WT and its corresponding location in ida4. In ida4, no densities are visible at this location as indicated by the blue dashed line. (View from the adjacent doublet microtubules. The proximal end of the axoneme is to the left.) (B) The structure of RS3S is unchanged in pf14 (purple), pf24 (turquoise), and pf1 (yellow) RS mutants. This indicates a different protein composition between RS3S and the other RSs. Bar, 25 nm.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3383722&req=5

Figure 5: Figure 5. 3D structure of Chlamydomonas RS3 stump (RS3S). (A) RS3S in WT (left) and ida4 (right) flagella. The RS3S is colored in orange and IDA d/a in blue. The IDA d/a is missing in ida4 flagella. The arrows show the approximate position of the dynein d/a tail in WT and its corresponding location in ida4. In ida4, no densities are visible at this location as indicated by the blue dashed line. (View from the adjacent doublet microtubules. The proximal end of the axoneme is to the left.) (B) The structure of RS3S is unchanged in pf14 (purple), pf24 (turquoise), and pf1 (yellow) RS mutants. This indicates a different protein composition between RS3S and the other RSs. Bar, 25 nm.
Mentions: Maybe the most surprising discovery of our cryo‐tomographic analysis of Chlamydomonas RSs was a short structure located at precisely the same place where RS3 is located in Tetrahymena (Figs. 2A, 3Aand5). The positioning and the morphological similarity between this short structure in Chlamydomonas and the reconstructed base of RS3 in Tetrahymena indicate that the Chlamydomonas repeat contains, in addition to the doublet of RS1 and RS2, a portion of the RS3.2 This finding was further confirmed by a comparison of the structure of Chlamydomonas with the structure of RS3 in sea urchin sperm flagella.45 We introduced the name RS3 stump (RS3S) for the portion of RS3 that is present in Chlamydomonas.

Bottom Line: Despite numerous biochemical, physiological and structural studies, the mechanism of the function of the radial spoke remains unclear.Detailed knowledge of the 3D structure of the RS protein complex is needed in order to understand how RS regulates dynein activity.Here we review the most important findings on the structure of the RS, including results of our recent cryo-electron tomographic analysis of the RS protein complex.

View Article: PubMed Central - PubMed

ABSTRACT
The radial spoke (RS) is a complex of at least 23 proteins that works as a mechanochemical transducer between the central-pair apparatus and the peripheral microtubule doublets in eukaryotic flagella and motile cilia. The RS contributes to the regulation of the activity of dynein motors, and thus to flagellar motility. Despite numerous biochemical, physiological and structural studies, the mechanism of the function of the radial spoke remains unclear. Detailed knowledge of the 3D structure of the RS protein complex is needed in order to understand how RS regulates dynein activity. Here we review the most important findings on the structure of the RS, including results of our recent cryo-electron tomographic analysis of the RS protein complex.

No MeSH data available.


Related in: MedlinePlus