Stabilization of sea urchin flagellar microtubules by histone H1.
Complex microtubule assemblies are essential components of eukaryotic cilia and flagella. They are extremely stable and are not affected by agents that normally induce polymer disassembly. The molecular basis of this microtubular stability is unknown, and it is not related to any feature of the constitutive tubulin. In sea urchin sperm flagella, axonemal microtubules are found to be stabilized by a protein identical to histone H1, a result that defines a new role for this histone and provides evidence for a concerted evolution of chromatin and microtubular structures.
Multigner
L
L
Département de Biologie Moléculaire et Structurale, Unité INSERM 244, Grenoble, France.
Gagnon
J
J
Van Dorsselaer
A
A
Job
D
D
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004305:Dose-Response Relationship, Drug; D006657:Histones / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D015151:Immunoblotting; D066298:In Vitro Techniques; D008297:Male; D008854:Microscopy, Electron; D008870:Microtubules / Q000187:drug effects*; D008969:Molecular Sequence Data; D012617:Sea Urchins; D017386:Sequence Homology, Amino Acid; D013082:Sperm Tail / Q000648:ultrastructure; D014404:Tubulin / Q000187:drug effects
D006657:Histones; D014404:Tubulin