scholarly journals Heme-binding protein CYB5D1 is a radial spoke component required for coordinated ciliary beating

2021 ◽  
Vol 118 (17) ◽  
pp. e2015689118
Author(s):  
Lijuan Zhao ◽  
Haibo Xie ◽  
Yunsi Kang ◽  
Yiwen Lin ◽  
Gai Liu ◽  
...  
Keyword(s):  
Redox State ◽  
Otic Vesicle ◽  
Heme Binding ◽  
Ciliary Beating ◽  
Radial Spoke ◽  
Slowing Down ◽  
Phototactic Response ◽  
Ciliary Protein ◽  
Biochemical Analyses ◽  
Heme Binding Protein

Coordinated beating is crucial for the function of multiple cilia. However, the molecular mechanism is poorly understood. Here, we characterize a conserved ciliary protein CYB5D1 with a heme-binding domain and a cordon-bleu ubiquitin-like domain. Mutation or knockdown of Cyb5d1 in zebrafish impaired coordinated ciliary beating in the otic vesicle and olfactory epithelium. Similarly, the two flagella of an insertional mutant of the CYB5D1 ortholog in Chlamydomonas (Crcyb5d1) showed an uncoordinated pattern due to a defect in the cis-flagellum. Biochemical analyses revealed that CrCYB5D1 is a radial spoke stalk protein that binds heme only under oxidizing conditions. Lack of CrCYB5D1 resulted in a reductive shift in flagellar redox state and slowing down of the phototactic response. Treatment of Crcyb5d1 with oxidants restored coordinated flagellar beating. Taken together, these data suggest that CrCYB5D1 may integrate environmental and intraciliary signals and regulate the redox state of cilia, which is crucial for the coordinated beating of multiple cilia.

scholarly journals Shigella dysenteriae ShuS Promotes Utilization of Heme as an Iron Source and Protects against Heme Toxicity

2005 ◽  
Vol 187 (16) ◽  
pp. 5658-5664 ◽  
Author(s):  
Elizabeth E. Wyckoff ◽  
Gregory F. Lopreato ◽  
Kimberly A. Tipton ◽  
Shelley M. Payne
Keyword(s):  
Bacillary Dysentery ◽  
Receptor Gene ◽  
Shigella Dysenteriae ◽  
Heme Binding ◽  
Anaerobic Conditions ◽  
Iron Source ◽  
Heme Transport ◽  
Serotype 1 ◽  
Increased Sensitivity ◽  
Heme Binding Protein

ABSTRACT Shigella dysenteriae serotype 1, a major cause of bacillary dysentery in humans, can use heme as a source of iron. Genes for the transport of heme into the bacterial cell have been identified, but little is known about proteins that control the fate of the heme molecule after it has entered the cell. The shuS gene is located within the heme transport locus, downstream of the heme receptor gene shuA. ShuS is a heme binding protein, but its role in heme utilization is poorly understood. In this work, we report the construction of a chromosomal shuS mutant. The shuS mutant was defective in utilizing heme as an iron source. At low heme concentrations, the shuS mutant grew slowly and its growth was stimulated by either increasing the heme concentration or by providing extra copies of the heme receptor shuA on a plasmid. At intermediate heme concentrations, the growth of the shuS mutant was moderately impaired, and at high heme concentrations, shuS was required for growth on heme. The shuS mutant did not show increased sensitivity to hydrogen peroxide, even at high heme concentrations. ShuS was also required for optimal utilization of heme under microaerobic and anaerobic conditions. These data are consistent with the model in which ShuS binds heme in a soluble, nontoxic form and potentially transfers the heme from the transport proteins in the membrane to either heme-containing or heme-degrading proteins. ShuS did not appear to store heme for future use.

Evolution of the SOUL Heme-Binding Protein Superfamily Across Eukarya

2016 ◽  
Vol 82 (6) ◽  
pp. 279-290 ◽  
Author(s):  
Antonio Emidio Fortunato ◽  
Paolo Sordino ◽  
Nikos Andreakis
Keyword(s):  
Binding Protein ◽  
Heme Binding ◽  
Protein Superfamily ◽  
Heme Binding Protein

DHR51, theDrosophila melanogasterHomologue of the Human Photoreceptor Cell-Specific Nuclear Receptor, Is a Thiolate Heme-Binding Protein†

Biochemistry ◽  
2008 ◽  
Vol 47 (50) ◽  
pp. 13252-13260 ◽  
Author(s):  
Eve de Rosny ◽  
Arjan de Groot ◽  
Celine Jullian-Binard ◽  
Franck Borel ◽  
Cristian Suarez ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Photoreceptor Cell ◽  
Binding Protein ◽  
Heme Binding ◽  
Heme Binding Protein

scholarly journals The Chlamydomonas IDA7 Locus Encodes a 140-kDa Dynein Intermediate Chain Required to Assemble the I1 Inner Arm Complex

1998 ◽  
Vol 9 (12) ◽  
pp. 3351-3365 ◽  
Author(s):  
Catherine A. Perrone ◽  
Pinfen Yang ◽  
Eileen O’Toole ◽  
Winfield S. Sale ◽  
Mary E. Porter
Keyword(s):  
Insertional Mutagenesis ◽  
Gene Transformation ◽  
Flagellar Motility ◽  
Wild Type ◽  
Gene Encoding ◽  
Radial Spoke ◽  
Important Target ◽  
Dynein Intermediate Chain ◽  
Biochemical Analyses ◽  
Intermediate Chain

To identify new loci that are involved in the assembly and targeting of dynein complexes, we have screened a collection of motility mutants that were generated by insertional mutagenesis. One such mutant, 5B10, lacks the inner arm isoform known as the I1 complex. This isoform is located proximal to the first radial spoke in each 96-nm axoneme repeat and is an important target for the regulation of flagellar motility. Complementation tests reveal that 5B10 represents a new I1 locus, IDA7. Biochemical analyses confirm thatida7 axonemes lack at least five I1 complex subunits. Southern blots probed with a clone containing the gene encoding the 140-kDa intermediate chain (IC) indicate that theida7 mutation is the result of plasmid insertion into the IC140 gene. Transformation with a wild-type copy of the IC140 gene completely rescues the mutant defects. Surprisingly, transformation with a construct of the IC140 gene lacking the first four exons of the coding sequence also rescues the mutant phenotype. These studies indicate that IC140 is essential for assembly of the I1 complex, but unlike other dynein ICs, the N-terminal region is not critical for its activity.

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