Molecular chaperones in cilia and flagella: Implications for protein turnover

✍ Scribed by Stephens, R.E. ;Lemieux, N.A.

• Publisher: John Wiley and Sons
• Year: 1999
• Tongue: English
• Weight: 217 KB
• Volume: 44
• Category: Article
• ISSN: 0886-1544
• DOI: 10.1002/(sici)1097-0169(199912)44:4<274::aid-cm5>3.0.co;2-o

✦ Synopsis

The mechanisms of protein incorporation and turnover in 9ϩ2 ciliary axonemes are not known. Previous reports of an HSP70-related protein, first in Chlamydomonas flagella and then in sea urchin embryonic cilia, suggested a potential role in protein transport or incorporation. The present study further explores this and other chaperones in axonemes from a representative range of organisms. Two-dimensional gel electrophoresis proved identity between the sea urchin ciliary 78 kDa HSP and a constitutive cytoplasmic HSP70 cognate (pI ϭ 5.71). When isolated flagella from mature sea urchin sperm were analyzed, the same total amount and distribution of 78 kDa protein as in cilia were found. Antigens of similar size were detected in ctenophore comb plate, molluscan gill, and rabbit tracheal cilia. Absent from sea urchin sperm flagella, TCP-1␣ was detected in sea urchin embryonic and rabbit tracheal cilia; the latter also contained HSP90, detected by two distinct antibodies. Tracheal cilia were shown to undergo axonemal protein turnover while tracheal cells mainly synthesized ciliary proteins. TCP-1␣ progressively appeared in regenerating embryonic cilia only as their growth slowed, suggesting a regulatory role in incorporation or turnover. These results demonstrate that chaperones are widely distributed ciliary and flagellar components, potentially related to axonemal protein dynamics.