The tau-like protein in silkworm (Bombyx mori) induces microtubule bundle formation

Front Biosci (Elite Ed). 2012 Jan 1;4(3):998-1008. doi: 10.2741/E435.

Abstract

Tau proteins are major microtubule-associated proteins (MAPs), which promote polymerization of tubulin and determine spacings between microtubules in axons of both the central and peripheral nervous systems (CNS and PNS). Here, we cloned and identified a tau-like protein BmTau from silkworm, Bombyx mori (GenBank accession number FJ904935). The coding sequence of BmTau is 723 bases long and encodes an approximate 30 kDa protein. In the C-terminus of BmTau are contained four predicted microtubule-binding domains, which share strong sequence homology to its ortholog in Drosophila melanoganster. Relative real-time PCR analysis showed ubiquitous expression of BmTau in both neurons and non-neural cells, with its mRNA abundantly expressing in brain but significantly less detected in trachea, fat body, and silkgland. Furthermore, immunocytochemical studies in BmN cells transfected with EGFP-BmTau indicated that BmTau functioned as microtubule bundling protein as its orthologues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Bombyx / metabolism*
  • Cells, Cultured
  • Cloning, Molecular
  • DNA Primers
  • DNA, Complementary
  • HeLa Cells
  • Humans
  • Microtubules / metabolism*
  • Molecular Sequence Data
  • Real-Time Polymerase Chain Reaction
  • Sequence Homology, Amino Acid
  • tau Proteins / genetics
  • tau Proteins / metabolism*

Substances

  • DNA Primers
  • DNA, Complementary
  • tau Proteins