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Open Access Highly Accessed Research article

The proline-rich domain of tau plays a role in interactions with actin

Hai Jin He12, Xing Sheng Wang2, Rong Pan2, Dong Liang Wang2, Ming Nan Liu1 and Rong Qiao He2*

Author Affiliations

1 State Key Laboratory of Brain and Cognitive Sciences, Institute of Biophysics, Key Lab of Mental Health, Institute of Psychology, Chinese Academy of Sciences, Beijing, PR China

2 Graduate University, Chinese Academy of Sciences, Beijing, PR China

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BMC Cell Biology 2009, 10:81  doi:10.1186/1471-2121-10-81

Published: 8 November 2009

Additional files

Additional file 1:

5'-, 3'- and M-primers used in PCR or megaprimer PCR amplification.

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Additional file 2:

Controls for co-sedimentation assays of actin incubated with tauPRD or tau. Conditions were the same as those for Figure 8, except that tauPRD, tauMTBD and tau were used in the absence of actin for co-sedimentation assays (panel a). F-actin with BSA (panel b) and actin alone (panel c) were employed as controls.

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Additional file 3:

Diameters of bundles and filaments of F-actin in the presence of tauPRD, tauMTBD and tau, determined using electron microscopy.

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Additional file 4:

Electron microscopic images of tauPRD, tauMTBD and tau. TauPRD, tauMTBD and tau were used as controls in the absence of actin.

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Additional file 5:

Analysis of the charge distribution of tau40. Arg and Lys are regarded as positively charged, and Asp and Glu as negatively charged. Thus, for the purposes of calculation, these four residues were considered as the charged components. Sequentially from the N- to the C-terminus, a window of 19 amino acid residues as a group was taken to calculate the average charge as described by Wang and coworkers [26]. Different regions of tau40 protein are indicated by different colours.

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Additional file 6:

Purification of tau and its mutants. Six truncated tau isolation and deletion mutants were constructed. Primers used were as shown in Additional file 1. Mutants were constructed as indicated (Figure 4). Mutants were expressed in E. coli and then purified through a Ni-NTA column. Samples were electrophoresed on a Tris-Tricine gel (panel b). Western blotting of tau mutants using monoclonal anti-His antibodies (panel b). Tau purified by Q-Sepharose and SP-Sepharose chromatography was analyzed by SDS-PAGE and western blotting using tau-13 anti-tau monoclonal antibodies (panel a).

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